1lns

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(New page: 200px<br /><applet load="1lns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lns, resolution 2.20&Aring;" /> '''Crystal Structure An...)
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[[Image:1lns.jpg|left|200px]]<br /><applet load="1lns" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lns, resolution 2.20&Aring;" />
caption="1lns, resolution 2.20&Aring;" />
'''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis'''<br />
'''Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis'''<br />
==Overview==
==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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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==
==About this Structure==
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1LNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LNS OCA].
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1LNS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNS OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xaa-Pro dipeptidyl-peptidase]]
[[Category: Xaa-Pro dipeptidyl-peptidase]]
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[[Category: Chich, J.F.]]
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[[Category: Chich, J F.]]
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[[Category: Delage, M.M.]]
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[[Category: Delage, M M.]]
[[Category: Mechin, I.]]
[[Category: Mechin, I.]]
[[Category: Rigolet, P.]]
[[Category: Rigolet, P.]]
[[Category: alpha beta hydrolase fold]]
[[Category: alpha beta hydrolase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:42:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:44 2008''

Revision as of 11:46, 21 February 2008


1lns, resolution 2.20Å

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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. Active as Xaa-Pro dipeptidyl-peptidase, with EC number 3.4.14.11 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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