Structural highlights
Function
[BTUC_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.[HAMAP-Rule:MF_01004] [BTUD_ECOLI] Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system (By similarity).
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
