2cbf
From Proteopedia
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THE X-RAY STRUCTURE OF A COBALAMIN BIOSYNTHETIC ENZYME, COBALT PRECORRIN-4 METHYLTRANSFERASE, CBIF, FROM BACILLUS MEGATERIUM, WITH THE HIS-TAG CLEAVED OFF
Overview
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.
About this Structure
2CBF is a Single protein structure of sequence from Bacillus megaterium with as ligand. Active as Precorrin-4 C(11)-methyltransferase, with EC number 2.1.1.133 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
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
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