2vjm: Difference between revisions

Revision as of 17:35, 27 July 2008

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File:2vjm.png

Template:STRUCTURE 2vjm

FORMYL-COA TRANSFERASE WITH ASPARTYL-FORMYL ANHYDIDE INTERMEDIATEFORMYL-COA TRANSFERASE WITH ASPARTYL-FORMYL ANHYDIDE INTERMEDIATE

Template:ABSTRACT PUBMED 18162462

About this StructureAbout this Structure

2VJM is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.

ReferenceReference

Reinvestigation of the Catalytic Mechanism of Formyl-CoA Transferase, a Class III CoA-transferase., Berthold CL, Toyota CG, Richards NG, Lindqvist Y, J Biol Chem. 2008 Mar 7;283(10):6519-29. Epub 2007 Dec 27. PMID:18162462

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2vjm|  PDB=2vjm  |  SCENE=  }}
-'''FORMYL-COA TRANSFERASE WITH ASPARTYL-FORMYL ANHYDIDE INTERMEDIATE'''
+===FORMYL-COA TRANSFERASE WITH ASPARTYL-FORMYL ANHYDIDE INTERMEDIATE===
-==Overview==
+<!--
-Formyl-coenzyme A transferase from Oxalobacter formigenes belongs to the Class III coenzyme A transferase family and catalyzes the reversible transfer of a CoA carrier between formyl-CoA and oxalate, forming oxalyl-CoA and formate. Formyl-CoA transferase has a unique three-dimensional fold composed of two interlaced subunits locked together like rings of a chain. We here present an intermediate in the reaction, formyl-CoA transferase containing the covalent beta-aspartyl-CoA thioester, adopting different conformations in the two active sites of the dimer, which was identified through crystallographic freeze-trapping experiments with formyl-CoA and oxalyl-CoA in the absence of acceptor carboxylic acid. The formation of the enzyme-CoA thioester was also confirmed by mass spectrometric data. Further structural data include a trapped aspartyl-formyl anhydride protected by a glycine loop closing down over the active site. In a crystal structure of the beta-aspartyl-CoA thioester of an inactive mutant variant, oxalate was found bound to the open conformation of the glycine loop. Together with hydroxylamine trapping experiments and kinetic as well as mutagenesis data, the structures of these formyl-CoA transferase complexes provide new information on the Class III CoA-transferase family and prompt redefinition of the catalytic steps and the modified reaction mechanism of formyl-CoA transferase proposed here.
+The line below this paragraph, {{ABSTRACT_PUBMED_18162462}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18162462 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18162462}}
 ==About this Structure==
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 [[Category: Cytoplasm]]
 [[Category: Transferase]]
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