2trm
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(New page: 200px<br /><applet load="2trm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2trm, resolution 2.8Å" /> '''THE THREE-DIMENSIONAL...)
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Revision as of 11:59, 21 November 2007
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THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS
Overview
The structure of the Asn102 mutant of trypsin was determined in order to, distinguish whether the reduced activity of the mutant at neutral pH, results from an altered active site conformation or from an inability to, stabilize a positive charge on the active site histidine. The active site, structure of the Asn102 mutant of trypsin is identical to the native, enzyme with respect to the specificity pocket, the oxyanion hole, and the, orientation of the nucleophilic serine. The observed decrease in rate, results from the loss of nucleophilicity of the active site serine. This, decreased nucleophilicity may result from stabilization of a His57, tautomer that is unable to accept the serine hydroxyl proton.
About this Structure
2TRM is a Single protein structure of sequence from Rattus norvegicus with CA and BEN as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis., Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS, Science. 1987 Aug 21;237(4817):905-9. PMID:3112942
Page seeded by OCA on Wed Nov 21 14:06:18 2007
