1lns

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{{STRUCTURE_1lns| PDB=1lns | SCENE= }}
{{STRUCTURE_1lns| PDB=1lns | SCENE= }}
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'''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis'''
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===Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12377124 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12377124}}
==About this Structure==
==About this Structure==
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[[Category: Rigolet, P.]]
[[Category: Rigolet, P.]]
[[Category: Alpha beta hydrolase fold]]
[[Category: Alpha beta hydrolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:05:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:31:08 2008''

Revision as of 18:31, 2 July 2008

Image:1lns.png

Template:STRUCTURE 1lns

Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

Template:ABSTRACT PUBMED 12377124

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

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