Ontology type: schema:ScholarlyArticle
2002-09
AUTHORSXiping Bi, Richard A. Corpina, Jonathan Goldberg
ABSTRACTCOPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1–GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24–Sar1 complex reveals a bow-tie-shaped structure, 15 nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis. More... »
PAGES271-277
http://scigraph.springernature.com/pub.10.1038/nature01040
DOIhttp://dx.doi.org/10.1038/nature01040
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1001233428
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/12239560
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/2008/06",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biological Sciences",
"type": "DefinedTerm"
},
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biochemistry and Cell Biology",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Amino Acid Sequence",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Binding Sites",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Biological Transport",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "COP-Coated Vesicles",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Crystallography, X-Ray",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Dimerization",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "GTPase-Activating Proteins",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Guanosine Diphosphate",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Guanosine Triphosphate",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Hydrolysis",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Macromolecular Substances",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Membrane Proteins",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Models, Molecular",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Molecular Sequence Data",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Monomeric GTP-Binding Proteins",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Binding",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Isoforms",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Structure, Secondary",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Structure, Tertiary",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Saccharomyces cerevisiae",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Saccharomyces cerevisiae Proteins",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Vesicular Transport Proteins",
"type": "DefinedTerm"
}
],
"author": [
{
"affiliation": {
"alternateName": "Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA",
"id": "http://www.grid.ac/institutes/grid.51462.34",
"name": [
"Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA"
],
"type": "Organization"
},
"familyName": "Bi",
"givenName": "Xiping",
"id": "sg:person.0661071645.54",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0661071645.54"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA",
"id": "http://www.grid.ac/institutes/grid.51462.34",
"name": [
"Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA"
],
"type": "Organization"
},
"familyName": "Corpina",
"givenName": "Richard A.",
"id": "sg:person.01137456156.79",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01137456156.79"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA",
"id": "http://www.grid.ac/institutes/grid.51462.34",
"name": [
"Howard Hughes Medical Institute and the Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021, New York, New York, USA"
],
"type": "Organization"
},
"familyName": "Goldberg",
"givenName": "Jonathan",
"id": "sg:person.0727205045.73",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0727205045.73"
],
"type": "Person"
}
],
"citation": [
{
"id": "sg:pub.10.1038/35078500",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1005889743",
"https://doi.org/10.1038/35078500"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/365347a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1031339056",
"https://doi.org/10.1038/365347a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/372704a0",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1006014539",
"https://doi.org/10.1038/372704a0"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/34438",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1047794485",
"https://doi.org/10.1038/34438"
],
"type": "CreativeWork"
},
{
"id": "sg:pub.10.1038/35043117",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1003610067",
"https://doi.org/10.1038/35043117"
],
"type": "CreativeWork"
}
],
"datePublished": "2002-09",
"datePublishedReg": "2002-09-01",
"description": "COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1\u2013GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation. Crystallographic analysis of the Saccharomyces cerevisiae Sec23/24\u2013Sar1 complex reveals a bow-tie-shaped structure, 15\u2009nm long, with a membrane-proximal surface that is concave and positively charged to conform to the size and acidic-phospholipid composition of the COPII vesicle. Sec23 and Sar1 form a continuous surface stabilized by a non-hydrolysable GTP analogue, and Sar1 has rearranged from the GDP conformation to expose amino-terminal residues that will probably embed in the bilayer. The GTPase-activating protein (GAP) activity of Sec23 involves an arginine side chain inserted into the Sar1 active site. These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis.",
"genre": "article",
"id": "sg:pub.10.1038/nature01040",
"isAccessibleForFree": false,
"isPartOf": [
{
"id": "sg:journal.1018957",
"issn": [
"0028-0836",
"1476-4687"
],
"name": "Nature",
"publisher": "Springer Nature",
"type": "Periodical"
},
{
"issueNumber": "6904",
"type": "PublicationIssue"
},
{
"type": "PublicationVolume",
"volumeNumber": "419"
}
],
"keywords": [
"COPII vesicle coat",
"GTP-dependent recruitment",
"pre-budding complexes",
"amino-terminal residues",
"Sar1-GTP",
"COPII vesicles",
"vesicle coat",
"arginine side chain",
"coat complex",
"coat polymerization",
"GTP hydrolysis",
"coat formation",
"stepwise recruitment",
"protein activity",
"structural basis",
"GDP conformation",
"endoplasmic reticulum",
"cytosolic components",
"cargo molecules",
"vesicles form",
"non-hydrolysable GTP analogue",
"membrane deformation",
"Sec23",
"GTP analogue",
"active site",
"side chains",
"recruitment",
"Sec13/31",
"Sec23/24",
"complexes",
"COPII",
"crystallographic analysis",
"GTPase",
"reticulum",
"snare",
"Sar1",
"vesicles",
"residues",
"conformation",
"coat",
"bilayers",
"hydrolysis",
"sites",
"molecules",
"shaped structure",
"structure",
"activity",
"composition",
"form",
"formation",
"chain",
"basis",
"components",
"analogues",
"analysis",
"size",
"observations",
"surface",
"polymerization",
"continuous surface",
"concave",
"deformation"
],
"name": "Structure of the Sec23/24\u2013Sar1 pre-budding complex of the COPII vesicle coat",
"pagination": "271-277",
"productId": [
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1001233428"
]
},
{
"name": "doi",
"type": "PropertyValue",
"value": [
"10.1038/nature01040"
]
},
{
"name": "pubmed_id",
"type": "PropertyValue",
"value": [
"12239560"
]
}
],
"sameAs": [
"https://doi.org/10.1038/nature01040",
"https://app.dimensions.ai/details/publication/pub.1001233428"
],
"sdDataset": "articles",
"sdDatePublished": "2022-08-04T16:54",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-springernature-scigraph/baseset/20220804/entities/gbq_results/article/article_357.jsonl",
"type": "ScholarlyArticle",
"url": "https://doi.org/10.1038/nature01040"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
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/nature01040'
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/nature01040'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/nature01040'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/nature01040'
This table displays all metadata directly associated to this object as RDF triples.
245 TRIPLES
21 PREDICATES
115 URIs
102 LITERALS
29 BLANK NODES