PDBsum entry 4jgi

Protein binding

PDB id: 4jgi

Contents

Protein chains

205 a.a.

Ligands

COB ×2

Waters ×421

PDB id:

4jgi

Name:

Protein binding

Title:

1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2

Structure:

Putative uncharacterized protein. Chain: a, b. Engineered: yes

Source:

Desulfitobacterium hafniense. Organism_taxid: 49338. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.50Å R-factor: 0.150 R-free: 0.194

Authors:

H.Sjuts,M.S.Dunstan,K.Fisher,D.Leys

Key ref:

H.Sjuts et al. (2013). Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2. Acta Crystallogr D Biol Crystallogr, 69, 1609-1616. PubMed id: 23897483 DOI: 10.1107/S0907444913011323

Date:

01-Mar-13 Release date: 07-Aug-13

Protein chains

Q8RPG0  (Q8RPG0_DESHA) -  Cobalamin-binding protein from Desulfitobacterium hafniense

Seq: 201 a.a.

Struc: 205 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444913011323

Acta Crystallogr D Biol Crystallogr 69:1609-1616 (2013)

PubMed id: 23897483

Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2.

H.Sjuts, M.S.Dunstan, K.Fisher, D.Leys.

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.