4JGI

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

Summary for 4JGI

• Entry DOI: 10.2210/pdb4jgi/pdb
• Descriptor: Putative uncharacterized protein, CO-METHYLCOBALAMIN (3 entities in total)
• Functional Keywords: rossmann fold, cobalamin binding, cobalamin, protein binding
• Biological source: Desulfitobacterium hafniense
• Total number of polymer chains: 2
• Total formula weight: 47804.27

Authors

Sjuts, H.,Dunstan, M.S.,Fisher, K.,Leys, D. (deposition date: 2013-03-01, release date: 2013-08-07, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)