3ci3 | pdb_00003ci3

Structure of the PduO-type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri complexed with partial adenosylcobalamin and PPPi

spinqualitylabelsall models 3ci3, resolution 1.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ci3 is a 1 chain structure with sequence from Lactobacillus reuteri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3PO, 5AD, B12, MG, NA Related: 2nt8, 3ci1, 3ci4 Gene: cobA (Lactobacillus reuteri) Activity: Cob(I)yrinic acid a,c-diamide adenosyltransferase, with EC number 2.5.1.17 Resources: FirstGlance, OCA, RCSB, PDBsum 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 ATP:cob(I)alamin adenosyltransferases (ACAs) catalyze the transfer of the 5'-deoxyadenosyl moiety from ATP to the upper axial ligand position of cobalamin in the synthesis of coenzyme B 12. For the ACA-catalyzed reaction to proceed, cob(II)alamin must be reduced to cob(I)alamin in the enzyme active site. This reduction is facilitated through the generation of a four-coordinate cob(II)alamin intermediate on the enzyme. We have determined the high-resolution crystal structure of a human-type ACA from Lactobacillus reuteri with a four-coordinate cob(II)alamin bound in the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site. The assembled structures represent snapshots of the steps in the ACA-catalyzed formation of the cobalt-carbon bond of coenzyme B 12. The structures define the corrinoid binding site and provide visual evidence for a base-off, four-coordinate cob(II)alamin intermediate. The complete structural description of ACA-mediated catalysis reveals the molecular features of four-coordinate cob(II)alamin stabilization and provides additional insights into the molecular basis for dysfunction in human patients suffering from methylmalonic aciduria. Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate.,St Maurice M, Mera P, Park K, Brunold TC, Escalante-Semerena JC, Rayment I Biochemistry. 2008 May 27;47(21):5755-66. Epub 2008 May 2. PMID:18452306 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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