Skip to Content
Merck
  • Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.

Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.

Nature structural & molecular biology (2014-11-18)
Vladimir M Korkhov, Samantha A Mireku, Dmitry B Veprintsev, Kaspar P Locher
PMID25402482
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.

MATERIALS
Product Number
Brand
Product Description
V2876
Sigma-Aldrich
Vitamin B12, ≥98%
V6629
Sigma-Aldrich
Vitamin B12, BioReagent, suitable for cell culture, suitable for insect cell culture, suitable for plant cell culture, ≥98%
47869
Supelco
Cyanocobalamin (B12), analytical standard
43107
Sigma-Aldrich
Cyanocobalamin, tested according to Ph. Eur.
C3607
Sigma-Aldrich
Cyanocobalamin, meets USP testing specifications
A2647
Sigma-Aldrich
Adenosine 5′-(β,γ-imido)triphosphate lithium salt hydrate, ≥93% (HPLC), powder
V-019
Supelco
Cyanocobalamin (Vitamin B12) solution, 1.0 mg/mL in methanol, ampule of 1 mL, certified reference material, Cerilliant®
C3000000
Cyanocobalamin, European Pharmacopoeia (EP) Reference Standard
PHR1234
Supelco
Cyanocobalamin, pharmaceutical secondary standard, certified reference material