1on3 | pdb_00001on3

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

spinqualitylabelsall models 1on3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1on3 is a 6 chain structure with sequence from "bacterium_acidi_propionici_a"_von_freudenreich_and_orla-jensen_1907 "bacterium acidi propionici a" von freudenreich and orla-jensen 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, DXX, MCA, MPD Related: 1on9 Activity: Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [12S_PROFR] The 12S subunit specifically catalyzes the transfer of the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit forming propanoyl-CoA and carboxylated 1.3S-biotin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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