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1on3

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{{STRUCTURE_1on3| PDB=1on3 | SCENE= }}
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'''Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)'''
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===Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)===
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==Overview==
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Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and oxaloacetate. The 1.9 A resolution crystal structure of the central 12S hexameric core, which catalyzes the first carboxylation reaction, has been solved bound to its substrate methylmalonyl-CoA. Overall, the structure reveals two stacked trimers related by 2-fold symmetry, and a domain duplication in the monomer. In the active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the N-termini of two alpha-helices. The 12S domains are structurally similar to the crotonase/isomerase superfamily, although only domain 1 of each 12S monomer binds ligand. The 12S reaction is similar to that of human propionyl-CoA carboxylase, whose beta-subunit has 50% sequence identity with 12S. A homology model of the propionyl-CoA carboxylase beta-subunit, based on this 12S crystal structure, provides new insight into the propionyl-CoA carboxylase mechanism, its oligomeric structure and the molecular basis of mutations responsible for enzyme deficiency in propionic acidemia.
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(as it appears on PubMed at http://www.pubmed.gov), where 12743028 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12743028}}
==About this Structure==
==About this Structure==
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[[Category: Multienzyme complex]]
[[Category: Multienzyme complex]]
[[Category: Transcarboxylase]]
[[Category: Transcarboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:09:05 2008''

Revision as of 20:09, 27 July 2008

Template:STRUCTURE 1on3

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)

Template:ABSTRACT PUBMED 12743028

About this Structure

1ON3 is a Single protein structure of sequence from Propionibacterium freudenreichii. Full crystallographic information is available from OCA.

Reference

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core., Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC, EMBO J. 2003 May 15;22(10):2334-47. PMID:12743028

Page seeded by OCA on Sun Jul 27 23:09:05 2008

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