1lns
From Proteopedia
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'''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis''' | '''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis''' | ||
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[[Category: Mechin, I.]] | [[Category: Mechin, I.]] | ||
[[Category: Rigolet, P.]] | [[Category: Rigolet, P.]] | ||
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Revision as of 21:05, 2 May 2008
Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis
Overview
The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis is a dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the N terminus of peptides. The structure of the enzyme was solved at 2.2 A resolution and provides a model for the peptidase family S15. Each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization. A C-terminal moiety probably plays a role in the tropism of X-PDAP toward the cellular membrane. These results give new insights for further exploration of the role of the enzymes of the SC clan.
About this Structure
1LNS is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
Reference
The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis., Rigolet P, Mechin I, Delage MM, Chich JF, Structure. 2002 Oct;10(10):1383-94. PMID:12377124 Page seeded by OCA on Sat May 3 00:05:42 2008
