4JGI

1.5 Angstrom crystal structure of a novel cobalamin-binding protein from Desulfitobacterium hafniense DCB-2

4JGI の概要

• エントリーDOI: 10.2210/pdb4jgi/pdb
• 分子名称: Putative uncharacterized protein, CO-METHYLCOBALAMIN (3 entities in total)
• 機能のキーワード: rossmann fold, cobalamin binding, cobalamin, protein binding
• 由来する生物種: Desulfitobacterium hafniense
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47804.27

構造登録者

Sjuts, H.,Dunstan, M.S.,Fisher, K.,Leys, D. (登録日: 2013-03-01, 公開日: 2013-08-07, 最終更新日: 2024-02-28)

主引用文献

Sjuts, H.,Dunstan, M.S.,Fisher, K.,Leys, D.
Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2.
Acta Crystallogr.,Sect.D, 69:1609-1616, 2013

PubMed Abstract: This study describes the identification and the structural and spectroscopic analysis of a cobalamin-binding protein (termed CobDH) implicated in O-demethylation by the organohalide-respiring bacterium Desulfitobacterium hafniense DCB-2. The 1.5 Å resolution crystal structure of CobDH is presented in the cobalamin-bound state and reveals that the protein is composed of an N-terminal helix-bundle domain and a C-terminal Rossmann-fold domain, with the cobalamin coordinated in the base-off/His-on conformation similar to other cobalamin-binding domains that catalyse methyl-transfer reactions. EPR spectroscopy of CobDH confirms cobalamin binding and reveals the presence of a cob(III)alamin superoxide, indicating binding of oxygen to the fully oxidized cofactor. These data provide the first structural insights into the methyltransferase reactions that occur during O-demethylation by D. hafniense.

PubMed: 23897483
DOI: 10.1107/S0907444913011323

実験手法

X-RAY DIFFRACTION (1.5 Å)