1CBF
THE X-RAY STRUCTURE OF A COBALAMIN BIOSYNTHETIC ENZYME, COBALT PRECORRIN-4 METHYLTRANSFERASE, CBIF
Summary for 1CBF
| Entry DOI | 10.2210/pdb1cbf/pdb |
| Descriptor | COBALT-PRECORRIN-4 TRANSMETHYLASE, PHOSPHATE ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total) |
| Functional Keywords | precorrin-4 methyltransferase, methylase, cobalamin biosynthesis, methyltransferase |
| Biological source | Bacillus megaterium |
| Total number of polymer chains | 1 |
| Total formula weight | 31570.40 |
| Authors | Schubert, H.L.,Raux, E.,Woodcock, S.C.,Wilson, K.S.,Warren, M.J. (deposition date: 1998-05-01, release date: 1999-05-11, Last modification date: 2024-02-07) |
| Primary citation | Schubert, H.L.,Wilson, K.S.,Raux, E.,Woodcock, S.C.,Warren, M.J. The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. Nat.Struct.Biol., 5:585-592, 1998 Cited by PubMed Abstract: 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. PubMed: 9665173DOI: 10.1038/846 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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