1dd2

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)

spinqualitylabelsall models 1dd2, 32 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dd2 is a 1 chain structure with sequence from "propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1dcz Activity: Methylmalonyl-CoA carboxytransferase, with EC number 2.1.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BCCP_PROFR] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits. 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 (TC) from Propionibacterium shermanii, a biotin-dependent enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and oxalacetate. Within the multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier and also binds the other two subunits to assist in the overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89. The three-dimensional solution structure of the full-length holo-1.3S subunit of TC has been solved by multidimensional heteronuclear NMR spectroscopy. The C-terminal half of the protein (51-123) is folded into a compact all-beta-domain comprising of two four-stranded antiparallel beta-sheets connected by short loops and turns. The fold exhibits a high 2-fold internal symmetry and is similar to that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the intact enzyme, appear to be disordered in the isolated 1.3S subunit. The molecular surface of the folded domain has two distinct surfaces: one side is highly charged, while the other comprises mainly hydrophobic, highly conserved residues. High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.,Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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