| Literature DB >> 25402482 |
Vladimir M Korkhov1, Samantha A Mireku2, Dmitry B Veprintsev3, Kaspar P Locher2.
Abstract
The reaction mechanism of BtuCD-F-catalyzed vitamin B12 transport into Escherichia coli is currently unclear. Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. Our structural and biochemical data allow a consistent mechanism to be formulated, thus rationalizing the roles of substrate, ATP and substrate-binding protein.Entities:
Mesh:
Substances:
Year: 2014 PMID: 25402482 DOI: 10.1038/nsmb.2918
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369