2ag1: Difference between revisions

Revision as of 14:57, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ag1.png

Template:STRUCTURE 2ag1

Crystal structure of Benzaldehyde lyase (BAL)- SeMetCrystal structure of Benzaldehyde lyase (BAL)- SeMet

Template:ABSTRACT PUBMED 16302970

About this StructureAbout this Structure

2AG1 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens., Mosbacher TG, Mueller M, Schulz GE, FEBS J. 2005 Dec;272(23):6067-76. PMID:16302970

Page seeded by OCA on Sun Jul 27 14:57:21 2008

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-'''Crystal structure of Benzaldehyde lyase (BAL)- SeMet'''
+===Crystal structure of Benzaldehyde lyase (BAL)- SeMet===
-==Overview==
+<!--
-Pseudomonas fluorescens is able to grow on R-benzoin as the sole carbon and energy source because it harbours the enzyme benzaldehyde lyase that cleaves the acyloin linkage using thiamine diphosphate (ThDP) as a cofactor. In the reverse reaction, this lyase catalyses the carboligation of two aldehydes with high substrate and stereospecificity. The enzyme structure was determined by X-ray diffraction at 2.6 A resolution. A structure-based comparison with other proteins showed that benzaldehyde lyase belongs to a group of closely related ThDP-dependent enzymes. The ThDP cofactors of these enzymes are fixed at their two ends in separate domains, suspending a comparatively mobile thiazolium ring between them. While the residues binding the two ends of ThDP are well conserved, the lining of the active centre pocket around the thiazolium moiety varies greatly within the group. Accounting for the known reaction chemistry, the natural substrate R-benzoin was modelled unambiguously into the active centre of the reported benzaldehyde lyase. Due to its substrate spectrum and stereospecificity, the enzyme extends the synthetic potential for carboligations appreciably.
+The line below this paragraph, {{ABSTRACT_PUBMED_16302970}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16302970}}
 ==About this Structure==
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 [[Category: Tetramer]]
 [[Category: Thdp dependent fold]]
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