2jet
From Proteopedia
(New page: 200px<br /><applet load="2jet" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jet, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
| - | The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has | + | The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has been determined at 2.2 A resolution. This mutant is the most trypsin-like mutant so far in the line of chymotrypsin-to-trypsin conversions, aiming for a more complete understanding of the structural basis of substrate specificity in pancreatic serine proteases. A226G caused significant rearrangements relative to S189D chymotrypsin, allowing an internal conformation of Asp189 which is close to that in trypsin. Serious distortions remain, however, in the activation domain, including zymogen-like features. The pH-profile of activity suggests that the conformation of the S1-site of the mutant is influenced also by the P1 residue of the substrate. |
==About this Structure== | ==About this Structure== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:02:34 2008'' |
Revision as of 16:02, 21 February 2008
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CRYSTAL STRUCTURE OF A TRYPSIN-LIKE MUTANT (S189D, A226G) CHYMOTRYPSIN.
Overview
The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has been determined at 2.2 A resolution. This mutant is the most trypsin-like mutant so far in the line of chymotrypsin-to-trypsin conversions, aiming for a more complete understanding of the structural basis of substrate specificity in pancreatic serine proteases. A226G caused significant rearrangements relative to S189D chymotrypsin, allowing an internal conformation of Asp189 which is close to that in trypsin. Serious distortions remain, however, in the activation domain, including zymogen-like features. The pH-profile of activity suggests that the conformation of the S1-site of the mutant is influenced also by the P1 residue of the substrate.
About this Structure
2JET is a Single protein structure of sequence from Rattus norvegicus. Active as Chymotrypsin, with EC number 3.4.21.1 Full crystallographic information is available from OCA.
Reference
The Crystal Structure of a Trypsin-like Mutant Chymotrypsin: The Role of Position 226 in the Activity and Specificity of S189D Chymotrypsin., Jelinek B, Katona G, Fodor K, Venekei I, Graf L, Protein J. 2007 Sep 6;. PMID:17805946
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