1pt5: Difference between revisions

Revision as of 17:52, 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:1pt5.png

Template:STRUCTURE 1pt5

Crystal structure of gene yfdW of E. coliCrystal structure of gene yfdW of E. coli

Template:ABSTRACT PUBMED 12844490

About this StructureAbout this Structure

1PT5 is a Single protein structure of sequence from Escherichia coli, and shigella flexneri. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases., Gruez A, Roig-Zamboni V, Valencia C, Campanacci V, Cambillau C, J Biol Chem. 2003 Sep 5;278(36):34582-6. Epub 2003 Jul 3. PMID:12844490

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OCA

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-'''Crystal structure of gene yfdW of E. coli'''
+===Crystal structure of gene yfdW of E. coli===
-==Overview==
+<!--
-Because of its toxicity, oxalate accumulation from amino acid catabolism leads to acute disorders in mammals. Gut microflora are therefore pivotal in maintaining a safe intestinal oxalate balance through oxalate degradation. Oxalate catabolism was first identified in Oxalobacter formigenes, a specialized, strictly anaerobic bacterium. Oxalate degradation was found to be performed successively by two enzymes, a formyl-CoA transferase (frc) and an oxalate decarboxylase (oxc). These two genes are present in several bacterial genomes including that of Escherichia coli. The frc ortholog in E. coli is yfdW, with which it shares 61% sequence identity. We have expressed the YfdW open reading frame product and solved its crystal structure in the apo-form and in complex with acetyl-CoA and with a mixture of acetyl-CoA and oxalate. YfdW exhibits a novel and spectacular fold in which two monomers assemble as interlaced rings, defining the CoA binding site at their interface. From the structure of the complex with acetyl-CoA and oxalate, we propose a putative formyl/oxalate transfer mechanism involving the conserved catalytic residue Asp169. The similarity of yfdW with bacterial orthologs (approximately 60% identity) and paralogs (approximately 20-30% identity) suggests that this new fold and parts of the CoA transfer mechanism are likely to be the hallmarks of a wide family of CoA transferases.
+The line below this paragraph, {{ABSTRACT_PUBMED_12844490}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12844490}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Transferase]]
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