2CBF

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

2CBF の概要

• エントリーDOI: 10.2210/pdb2cbf/pdb
• 分子名称: COBALT-PRECORRIN-4 TRANSMETHYLASE, S-ADENOSYL-L-HOMOCYSTEINE (2 entities in total)
• 機能のキーワード: precorrin-4 methyltransferase, methylase, cobalamin biosynthesis, methyltransferase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25889.24

構造登録者

Schubert, H.L.,Raux, E.,Woodcock, S.C.,Warren, M.J.,Wilson, K.S. (登録日: 1998-05-01, 公開日: 1999-05-11, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.1 Å)