Three-dimensional Structure of Tosyl-α-chymotrypsin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1967-05

AUTHORS

B. W. MATTHEWS, P. B. SIGLER, R. HENDERSON, D. M. BLOW

ABSTRACT

A model is proposed for the structure of an inhibited derivative of an enzyme which hydrolyses proteins. It is based on a map of the electron density distribution at 2 Å resolution and interpreted in terms of a previously reported sequence of 241 amino-acids. The map has been derived from a Fourier synthesis of 24,500 terms and represents two crystallographically independent molecules, each of molecular weight 25,000, which are nearly identical in their tertiary structure. The enzyme is composed almost entirely of extended polypeptide chains. A chemical marker unambiguously defines the position of the active centre. The position and orientation of the residues known to be important in catalysis are clearly seen. The mechanism by which the inactive precursor is converted into an active enzyme is revealed. More... »

PAGES

652-656

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/214652a0

DOI

http://dx.doi.org/10.1038/214652a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013716055

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6049071


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/03", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Chemical Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0306", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Physical Chemistry (incl. Structural)", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Amino Acid Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Chemical Phenomena", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Chemistry", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Chymotrypsin", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Crystallography", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Structural", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Peptides", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "X-Ray Diffraction", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Laboratory of Molecular Biology, NIAMID, 20014, Bethesda, Maryland, U.S.A.", 
          "id": "http://www.grid.ac/institutes/None", 
          "name": [
            "M.R.C. Laboratory of Molecular Biology, Cambridge, England", 
            "Laboratory of Molecular Biology, NIAMID, 20014, Bethesda, Maryland, U.S.A."
          ], 
          "type": "Organization"
        }, 
        "familyName": "MATTHEWS", 
        "givenName": "B. W.", 
        "id": "sg:person.0105144750.25", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0105144750.25"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "M.R.C. Laboratory of Molecular Biology, Cambridge, England", 
          "id": "http://www.grid.ac/institutes/grid.42475.30", 
          "name": [
            "M.R.C. Laboratory of Molecular Biology, Cambridge, England"
          ], 
          "type": "Organization"
        }, 
        "familyName": "SIGLER", 
        "givenName": "P. B.", 
        "id": "sg:person.075656371.77", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.075656371.77"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "M.R.C. Laboratory of Molecular Biology, Cambridge, England", 
          "id": "http://www.grid.ac/institutes/grid.42475.30", 
          "name": [
            "M.R.C. Laboratory of Molecular Biology, Cambridge, England"
          ], 
          "type": "Organization"
        }, 
        "familyName": "HENDERSON", 
        "givenName": "R.", 
        "id": "sg:person.01370477602.99", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01370477602.99"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "M.R.C. Laboratory of Molecular Biology, Cambridge, England", 
          "id": "http://www.grid.ac/institutes/grid.42475.30", 
          "name": [
            "M.R.C. Laboratory of Molecular Biology, Cambridge, England"
          ], 
          "type": "Organization"
        }, 
        "familyName": "BLOW", 
        "givenName": "D. M.", 
        "id": "sg:person.01103546737.09", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01103546737.09"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/190666a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1039647388", 
          "https://doi.org/10.1038/190666a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/2011284a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1021701870", 
          "https://doi.org/10.1038/2011284a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/213862a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1038405748", 
          "https://doi.org/10.1038/213862a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/141523a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1012499119", 
          "https://doi.org/10.1038/141523a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/206757a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050588896", 
          "https://doi.org/10.1038/206757a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1967-05", 
    "datePublishedReg": "1967-05-01", 
    "description": "A model is proposed for the structure of an inhibited derivative of an enzyme which hydrolyses proteins. It is based on a map of the electron density distribution at 2 \u00c5 resolution and interpreted in terms of a previously reported sequence of 241 amino-acids. The map has been derived from a Fourier synthesis of 24,500 terms and represents two crystallographically independent molecules, each of molecular weight 25,000, which are nearly identical in their tertiary structure. The enzyme is composed almost entirely of extended polypeptide chains. A chemical marker unambiguously defines the position of the active centre. The position and orientation of the residues known to be important in catalysis are clearly seen. The mechanism by which the inactive precursor is converted into an active enzyme is revealed.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/214652a0", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1018957", 
        "issn": [
          "0028-0836", 
          "1476-4687"
        ], 
        "name": "Nature", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "5089", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "214"
      }
    ], 
    "keywords": [
      "electron density distribution", 
      "independent molecules", 
      "active center", 
      "chemical markers", 
      "molecular weight", 
      "Fourier synthesis", 
      "three-dimensional structure", 
      "tertiary structure", 
      "polypeptide chain", 
      "active enzyme", 
      "catalysis", 
      "structure", 
      "density distribution", 
      "synthesis", 
      "molecules", 
      "derivatives", 
      "enzyme", 
      "precursors", 
      "tosyl", 
      "chain", 
      "chymotrypsin", 
      "residues", 
      "inactive precursor", 
      "orientation", 
      "position", 
      "mechanism", 
      "protein", 
      "resolution", 
      "weight", 
      "sequence", 
      "terms", 
      "center", 
      "distribution", 
      "markers", 
      "maps", 
      "model", 
      "inhibited derivative"
    ], 
    "name": "Three-dimensional Structure of Tosyl-\u03b1-chymotrypsin", 
    "pagination": "652-656", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1013716055"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/214652a0"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "6049071"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/214652a0", 
      "https://app.dimensions.ai/details/publication/pub.1013716055"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-01-01T19:03", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220101/entities/gbq_results/article/article_96.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/214652a0"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/214652a0'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/214652a0'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/214652a0'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/214652a0'


 

This table displays all metadata directly associated to this object as RDF triples.

175 TRIPLES      21 PREDICATES      76 URIs      63 LITERALS      15 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/214652a0 schema:about N33e867a2c4894f15991b04db0cdc57f2
2 N45eda65913e84d9ca8d36fdc073947d3
3 N7aa3bd8095594d52b098e7d8d9511957
4 Nadd66087a5374fbdb7215b89aa36f952
5 Nd6a819269a264bcc90cb645cd1211dd4
6 Ndc941b9235e84e9389462189653fcd90
7 Nf90c289899ae492ca476d1edb0d81dfa
8 Nf92f5b29ef2b4af6bc06ad2763083a7d
9 anzsrc-for:03
10 anzsrc-for:0306
11 schema:author N74b6b2bb89d447ecbf826a91591a4da4
12 schema:citation sg:pub.10.1038/141523a0
13 sg:pub.10.1038/190666a0
14 sg:pub.10.1038/2011284a0
15 sg:pub.10.1038/206757a0
16 sg:pub.10.1038/213862a0
17 schema:datePublished 1967-05
18 schema:datePublishedReg 1967-05-01
19 schema:description A model is proposed for the structure of an inhibited derivative of an enzyme which hydrolyses proteins. It is based on a map of the electron density distribution at 2 Å resolution and interpreted in terms of a previously reported sequence of 241 amino-acids. The map has been derived from a Fourier synthesis of 24,500 terms and represents two crystallographically independent molecules, each of molecular weight 25,000, which are nearly identical in their tertiary structure. The enzyme is composed almost entirely of extended polypeptide chains. A chemical marker unambiguously defines the position of the active centre. The position and orientation of the residues known to be important in catalysis are clearly seen. The mechanism by which the inactive precursor is converted into an active enzyme is revealed.
20 schema:genre article
21 schema:isAccessibleForFree false
22 schema:isPartOf N656592e981884e40a29c526a0342c7da
23 Nf00e5e104ea045c391b489f583190183
24 sg:journal.1018957
25 schema:keywords Fourier synthesis
26 active center
27 active enzyme
28 catalysis
29 center
30 chain
31 chemical markers
32 chymotrypsin
33 density distribution
34 derivatives
35 distribution
36 electron density distribution
37 enzyme
38 inactive precursor
39 independent molecules
40 inhibited derivative
41 maps
42 markers
43 mechanism
44 model
45 molecular weight
46 molecules
47 orientation
48 polypeptide chain
49 position
50 precursors
51 protein
52 residues
53 resolution
54 sequence
55 structure
56 synthesis
57 terms
58 tertiary structure
59 three-dimensional structure
60 tosyl
61 weight
62 schema:name Three-dimensional Structure of Tosyl-α-chymotrypsin
63 schema:pagination 652-656
64 schema:productId N98367dfe7ff14d4c8eed983e7b8edf96
65 N9cbf5074a5534be4843f6f4f6b3518d1
66 Nf7468a75fd474a0a95008e73ac38f73f
67 schema:sameAs https://app.dimensions.ai/details/publication/pub.1013716055
68 https://doi.org/10.1038/214652a0
69 schema:sdDatePublished 2022-01-01T19:03
70 schema:sdLicense https://scigraph.springernature.com/explorer/license/
71 schema:sdPublisher Nef3fea2c8c21400cbfb84acc29435036
72 schema:url https://doi.org/10.1038/214652a0
73 sgo:license sg:explorer/license/
74 sgo:sdDataset articles
75 rdf:type schema:ScholarlyArticle
76 N33e867a2c4894f15991b04db0cdc57f2 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
77 schema:name Amino Acid Sequence
78 rdf:type schema:DefinedTerm
79 N45eda65913e84d9ca8d36fdc073947d3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
80 schema:name Crystallography
81 rdf:type schema:DefinedTerm
82 N4efb1d667ffa4d968740fd564cfd6cdc rdf:first sg:person.01103546737.09
83 rdf:rest rdf:nil
84 N656592e981884e40a29c526a0342c7da schema:issueNumber 5089
85 rdf:type schema:PublicationIssue
86 N74b6b2bb89d447ecbf826a91591a4da4 rdf:first sg:person.0105144750.25
87 rdf:rest N99ea69193e974f7580d2cf9425cdb6f5
88 N7aa3bd8095594d52b098e7d8d9511957 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
89 schema:name Chymotrypsin
90 rdf:type schema:DefinedTerm
91 N848da14744bd4917a40bdc45e5d50c3a rdf:first sg:person.01370477602.99
92 rdf:rest N4efb1d667ffa4d968740fd564cfd6cdc
93 N98367dfe7ff14d4c8eed983e7b8edf96 schema:name dimensions_id
94 schema:value pub.1013716055
95 rdf:type schema:PropertyValue
96 N99ea69193e974f7580d2cf9425cdb6f5 rdf:first sg:person.075656371.77
97 rdf:rest N848da14744bd4917a40bdc45e5d50c3a
98 N9cbf5074a5534be4843f6f4f6b3518d1 schema:name doi
99 schema:value 10.1038/214652a0
100 rdf:type schema:PropertyValue
101 Nadd66087a5374fbdb7215b89aa36f952 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
102 schema:name X-Ray Diffraction
103 rdf:type schema:DefinedTerm
104 Nd6a819269a264bcc90cb645cd1211dd4 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
105 schema:name Chemical Phenomena
106 rdf:type schema:DefinedTerm
107 Ndc941b9235e84e9389462189653fcd90 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
108 schema:name Chemistry
109 rdf:type schema:DefinedTerm
110 Nef3fea2c8c21400cbfb84acc29435036 schema:name Springer Nature - SN SciGraph project
111 rdf:type schema:Organization
112 Nf00e5e104ea045c391b489f583190183 schema:volumeNumber 214
113 rdf:type schema:PublicationVolume
114 Nf7468a75fd474a0a95008e73ac38f73f schema:name pubmed_id
115 schema:value 6049071
116 rdf:type schema:PropertyValue
117 Nf90c289899ae492ca476d1edb0d81dfa schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
118 schema:name Peptides
119 rdf:type schema:DefinedTerm
120 Nf92f5b29ef2b4af6bc06ad2763083a7d schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
121 schema:name Models, Structural
122 rdf:type schema:DefinedTerm
123 anzsrc-for:03 schema:inDefinedTermSet anzsrc-for:
124 schema:name Chemical Sciences
125 rdf:type schema:DefinedTerm
126 anzsrc-for:0306 schema:inDefinedTermSet anzsrc-for:
127 schema:name Physical Chemistry (incl. Structural)
128 rdf:type schema:DefinedTerm
129 sg:journal.1018957 schema:issn 0028-0836
130 1476-4687
131 schema:name Nature
132 schema:publisher Springer Nature
133 rdf:type schema:Periodical
134 sg:person.0105144750.25 schema:affiliation grid-institutes:None
135 schema:familyName MATTHEWS
136 schema:givenName B. W.
137 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0105144750.25
138 rdf:type schema:Person
139 sg:person.01103546737.09 schema:affiliation grid-institutes:grid.42475.30
140 schema:familyName BLOW
141 schema:givenName D. M.
142 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01103546737.09
143 rdf:type schema:Person
144 sg:person.01370477602.99 schema:affiliation grid-institutes:grid.42475.30
145 schema:familyName HENDERSON
146 schema:givenName R.
147 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01370477602.99
148 rdf:type schema:Person
149 sg:person.075656371.77 schema:affiliation grid-institutes:grid.42475.30
150 schema:familyName SIGLER
151 schema:givenName P. B.
152 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.075656371.77
153 rdf:type schema:Person
154 sg:pub.10.1038/141523a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1012499119
155 https://doi.org/10.1038/141523a0
156 rdf:type schema:CreativeWork
157 sg:pub.10.1038/190666a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1039647388
158 https://doi.org/10.1038/190666a0
159 rdf:type schema:CreativeWork
160 sg:pub.10.1038/2011284a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1021701870
161 https://doi.org/10.1038/2011284a0
162 rdf:type schema:CreativeWork
163 sg:pub.10.1038/206757a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1050588896
164 https://doi.org/10.1038/206757a0
165 rdf:type schema:CreativeWork
166 sg:pub.10.1038/213862a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1038405748
167 https://doi.org/10.1038/213862a0
168 rdf:type schema:CreativeWork
169 grid-institutes:None schema:alternateName Laboratory of Molecular Biology, NIAMID, 20014, Bethesda, Maryland, U.S.A.
170 schema:name Laboratory of Molecular Biology, NIAMID, 20014, Bethesda, Maryland, U.S.A.
171 M.R.C. Laboratory of Molecular Biology, Cambridge, England
172 rdf:type schema:Organization
173 grid-institutes:grid.42475.30 schema:alternateName M.R.C. Laboratory of Molecular Biology, Cambridge, England
174 schema:name M.R.C. Laboratory of Molecular Biology, Cambridge, England
175 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...