2h9d: Difference between revisions

Revision as of 00:43, 28 July 2008

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File:2h9d.png

Template:STRUCTURE 2h9d

Pyruvate-Bound Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aerugionsaPyruvate-Bound Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aerugionsa

Template:ABSTRACT PUBMED 16914555

About this StructureAbout this Structure

2H9D is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa., Zaitseva J, Lu J, Olechoski KL, Lamb AL, J Biol Chem. 2006 Nov 3;281(44):33441-9. Epub 2006 Aug 16. PMID:16914555

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OCA

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-'''Pyruvate-Bound Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aerugionsa'''
+===Pyruvate-Bound Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aerugionsa===
-==Overview==
+<!--
-Enzymatic systems that exploit pericyclic reaction mechanisms are rare. A recent addition to this class is the enzyme PchB, an 11.4-kDa isochorismate pyruvate lyase from Pseudomonas aeruginosa. The apo and pyruvate-bound structures of PchB reveal that the enzyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence identity (20%). The enzyme is an intertwined dimer of three helices with connecting loops, and amino acids from each monomer participate in each of two active sites. The apo structure (2.35 A resolution) has one dimer per asymmetric unit with nitrate bound in an open active site. The loop between the first and second helices is disordered, providing a gateway for substrate entry and product exit. The pyruvate-bound structure (1.95 A resolution) has two dimers per asymmetric unit. One has two open active sites like the apo structure, and the other has two closed active sites with the loop between the first and second helices ordered for catalysis. Determining the structure of PchB is part of a larger effort to elucidate protein structures involved in siderophore biosynthesis, as these enzymes are crucial for bacterial iron uptake and virulence and have been identified as antimicrobial drug targets.
+The line below this paragraph, {{ABSTRACT_PUBMED_16914555}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16914555}}
 ==About this Structure==
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 [[Category: Zaitseva, J.]]
 [[Category: Intertwined dimer]]
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