1lns
From Proteopedia
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- | [[Image:1lns.jpg|left|200px]] | + | [[Image:1lns.jpg|left|200px]] |
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- | '''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis''' | + | {{Structure |
+ | |PDB= 1lns |SIZE=350|CAPTION= <scene name='initialview01'>1lns</scene>, resolution 2.20Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidyl-peptidase Xaa-Pro dipeptidyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.11 3.4.14.11] | ||
+ | |GENE= pepX (ORF2) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1LNS is a [ | + | 1LNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12377124 12377124] |
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha beta hydrolase fold]] | [[Category: alpha beta hydrolase fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:04 2008'' |
Revision as of 10:33, 20 March 2008
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, resolution 2.20Å | |||||||
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Gene: | pepX (ORF2) (Lactococcus lactis) | ||||||
Activity: | Xaa-Pro dipeptidyl-peptidase, with EC number 3.4.14.11 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
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