1on3
From Proteopedia
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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)''' | '''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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[[Category: Yee, V C.]] | [[Category: Yee, V C.]] | ||
[[Category: Zheng, X.]] | [[Category: Zheng, X.]] | ||
| - | [[Category: | + | [[Category: Carboxyl transferase]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Domain duplication]] |
| - | [[Category: | + | [[Category: Multienzyme complex]] |
| - | [[Category: | + | [[Category: Transcarboxylase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:03:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:03, 3 May 2008
Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound)
Overview
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.
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 Sat May 3 04:03:09 2008
Categories: Methylmalonyl-CoA carboxytransferase | Propionibacterium freudenreichii | Single protein | Carey, P R. | Hall, P R. | Pustai-Carey, M. | Rivera-Hainaj, R E. | Wang, Y F. | Yee, V C. | Zheng, X. | Carboxyl transferase | Crystal structure | Domain duplication | Multienzyme complex | Transcarboxylase
