2bkl

From Proteopedia

Revision as of 14:35, 30 October 2007

STRUCTURAL AND MECHANISTIC ANALYSIS OF TWO PROLYL ENDOPEPTIDASES: ROLE OF INTER-DOMAIN DYNAMICS IN CATALYSIS AND SPECIFICITY

Overview

Prolyl endopeptidases (PEPs) are a unique class of serine proteases with, considerable therapeutic potential for the treatment of celiac sprue. The, crystal structures of two didomain PEPs have been solved in alternative, configurations, thereby providing insights into the mode of action of, these enzymes. The structure of the Sphingomonas capsulata PEP, solved and, refined to 1.8-A resolution, revealed an open configuration of the active, site. In contrast, the inhibitor-bound PEP from Myxococcus xanthus was, crystallized (1.5-A resolution) in a closed form. Comparative analysis of, the two structures highlights a critical role for the domain interface in, regulating interdomain dynamics and substrate specificity. Structure-based, mutagenesis of the M. xanthus PEP confirms an important ... [(full description)]

About this Structure

2BKL is a [Single protein] structure of sequence from [Myxococcus xanthus] with SO4, ZAH and MES as [ligands]. Active as [Prolyl oligopeptidase], with EC number [3.4.21.26]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Structural and mechanistic analysis of two prolyl endopeptidases: role of interdomain dynamics in catalysis and specificity., Shan L, Mathews II, Khosla C, Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3599-604. Epub 2005 Feb 28. PMID:15738423

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