2bkl
From Proteopedia
(New page: 200px<br /> <applet load="2bkl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bkl, resolution 1.50Å" /> '''STRUCTURAL AND MECH...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BKL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]] with SO4, ZAH and MES as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BKL OCA]]. | + | 2BKL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]] with SO4, ZAH and MES as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BKL OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15738423 15738423] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15738423 15738423] | ||
[[Category: Myxococcus xanthus]] | [[Category: Myxococcus xanthus]] | ||
| + | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Khosla, C.]] | [[Category: Khosla, C.]] | ||
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[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:06:25 2007'' |
Revision as of 12:01, 30 October 2007
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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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