Structural highlights
Publication Abstract from PubMed
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.
Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.,Korkhov VM, Mireku SA, Veprintsev DB, Locher KP Nat Struct Mol Biol. 2014 Nov 17. doi: 10.1038/nsmb.2918. PMID:25402482[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Korkhov VM, Mireku SA, Veprintsev DB, Locher KP. Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F. Nat Struct Mol Biol. 2014 Nov 17. doi: 10.1038/nsmb.2918. PMID:25402482 doi:http://dx.doi.org/10.1038/nsmb.2918
