Ribonucleases A and T1 Comparable Mechanisms of RNA Cleavage with Different Active Site Geometries View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

W. Saenger , R. Arni , M. Maslowska , A. Pähler , U. Heinemann

ABSTRACT

There are a variety of enzymes which cleave the phosphodiester link in ribo- and deoxyribonucleic acids. They exhibit different catalytic activities, different mechanisms of cleavage, and different three-dimensional structures. The best known examples are DNase I which acts upon single and double stranded DNA , staphylococcal nuclease which cleaves P-0 bonds in RNA and DNA single strands2 , and the two RNases A and T1 which cut at the 3′-end of pyrimidine and guanosine nucleotides respectively3-5 . Although the two RNases have different molecular topology, the mechanism of hydrolysis is similar and suggestive of a comparable active site geometry. Since high resolution crystal structures are available (1.5Å for RNase A and 2.oÅ for RNase T1)3-5, a study of the arrangement of the functional amino acids in the1 active sites of the two enzymes is of interest. More... »

PAGES

337-344

Book

TITLE

Crystallography in Molecular Biology

ISBN

978-1-4684-5274-7
978-1-4684-5272-3

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4684-5272-3_29

DOI

http://dx.doi.org/10.1007/978-1-4684-5272-3_29

DIMENSIONS

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