1cbf | pdb_00001cbf

THE X-RAY STRUCTURE OF A COBALAMIN BIOSYNTHETIC ENZYME, COBALT PRECORRIN-4 METHYLTRANSFERASE, CBIF

spinqualitylabelsall models 1cbf, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cbf is a 1 chain structure with sequence from Atcc 14581. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4, SAH Gene: CBIF (ATCC 14581) Activity: Precorrin-4 C(11)-methyltransferase, with EC number 2.1.1.133 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [CBIF_BACME] Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A. 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 Biosynthesis of the corrin ring of vitamin B12 requires the action of six S-adenosyl-L-methionine (AdoMet) dependent transmethylases, closely related in sequence. The first X-ray structure of one of these, cobalt-precorrin-4 transmethylase, CbiF, from Bacillus megaterium has been determined to a resolution of 2.4 A. CbiF contains two alphabeta domains forming a trough in which S-adenosyl-L-homocysteine (AdoHcy) binds. The location of AdoHcy and a number of conserved residues, helps define the precorrin binding site. A second crystal form determined at 3.1 A resolution highlights the flexibility of two loops around this site. CbiF employs a unique mode of AdoHcy binding and represents a new class of transmethylase. The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase.,Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ Nat Struct Biol. 1998 Jul;5(7):585-92. PMID:9665173 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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