1rra
From Proteopedia
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RIBONUCLEASE A FROM RATTUS NORVEGICUS (COMMON RAT)
Overview
The three-dimensional structure of rat pancreatic RNase A expressed in, Escherichia coli was determined. The backbone conformations of certain, critical loops are significantly different in this enzyme compared to its, bovine counterpart. However, the core structure of rat RNase A is similar, to that of the other members of the pancreatic ribonuclease family. The, structural variations within a loop bordering the active site can be, correlated with the subtle differences in the enzymatic activities of, bovine and rat ribonucleases for different substrates. The most, significant difference in the backbone conformation was observed in the, loop 15-25. This loop incorporates the subtilisin cleavage site which is, responsible for RNase A to RNase S conversion in the bovine enzyme. The, rat enzyme does not get cleaved under identical conditions. Molecular, docking of this region of the rat enzyme in the active site of subtilisin, shows steric incompatibility, although the bovine pancreatic ribonuclease, A appropriately fits into this active site. It is therefore inferred that, the local conformation of the substrate governs the specificity of, subtilisin.
About this Structure
1RRA is a Single protein structure of sequence from Rattus norvegicus with PO4 as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
Reference
The crystal structure of recombinant rat pancreatic RNase A., Gupta V, Muyldermans S, Wyns L, Salunke DM, Proteins. 1999 Apr 1;35(1):1-12. PMID:10090281
Page seeded by OCA on Wed Nov 21 01:48:55 2007
