4jgi

Publication Abstract from PubMed

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 A 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.

Structure of the cobalamin-binding protein of a putative O-demethylase from Desulfitobacterium hafniense DCB-2.,Sjuts H, Dunstan MS, Fisher K, Leys D Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1609-16. doi:, 10.1107/S0907444913011323. Epub 2013 Jul 20. PMID:23897483^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.