4R9U

Structure of vitamin B12 transporter BtuCD in a nucleotide-bound outward facing state

Summary for 4R9U

• Entry DOI: 10.2210/pdb4r9u/pdb
• Descriptor: Vitamin B12 import system permease protein BtuC, Vitamin B12 import ATP-binding protein BtuD, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total)
• Functional Keywords: nucleotide, amppnp, atp binding cassette, membrane protein, abc transporter, btuf, inner membrane, hydrolase
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P06609; Cell inner membrane; Peripheral membrane protein: P06611
• Total number of polymer chains: 4
• Total formula weight: 127119.51

Authors

Korkhov, V.M.,Mireku, S.A.,Veprintsev, D.B.,Locher, K.P. (deposition date: 2014-09-08, release date: 2014-11-19, Last modification date: 2024-11-20)

Primary citation

Korkhov, V.M.,Mireku, S.A.,Veprintsev, D.B.,Locher, K.P.
Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.
Nat.Struct.Mol.Biol., 21:1097-1099, 2014

PubMed 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.

PubMed: 25402482
DOI: 10.1038/nsmb.2918

Experimental method

X-RAY DIFFRACTION (2.785 Å)