2CBF

THE X-RAY STRUCTURE OF A COBALAMIN BIOSYNTHETIC ENZYME, COBALT PRECORRIN-4 METHYLTRANSFERASE, CBIF, FROM BACILLUS MEGATERIUM, WITH THE HIS-TAG CLEAVED OFF

Summary for 2CBF

• Entry DOI: 10.2210/pdb2cbf/pdb
• Descriptor: COBALT-PRECORRIN-4 TRANSMETHYLASE, S-ADENOSYL-L-HOMOCYSTEINE (2 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: 25889.24

Authors

Schubert, H.L.,Raux, E.,Woodcock, S.C.,Warren, M.J.,Wilson, K.S. (deposition date: 1998-05-01, release date: 1999-05-11, Last modification date: 2024-04-03)

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

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: 9665173
DOI: 10.1038/846

Experimental method

X-RAY DIFFRACTION (3.1 Å)