4DBL

Crystal structure of E159Q mutant of BtuCDF

Summary for 4DBL

• Entry DOI: 10.2210/pdb4dbl/pdb
• Descriptor: Vitamin B12 import system permease protein BtuC, Vitamin B12 import ATP-binding protein BtuD, Vitamin B12-binding protein, ... (5 entities in total)
• Functional Keywords: abc transporter for vitamin b12, atp binding, inner membrane, transport protein
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P06609; Cell inner membrane; Peripheral membrane protein: P06611; Periplasm: P37028
• Total number of polymer chains: 10
• Total formula weight: 316999.84

Authors

Korkhov, V.M.,Mireku, S.M.,Hvorup, R.N.,Locher, K.P. (deposition date: 2012-01-16, release date: 2012-03-07, Last modification date: 2024-10-30)

Primary citation

Korkhov, V.M.,Mireku, S.A.,Hvorup, R.N.,Locher, K.P.
Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF.
Febs Lett., 586:972-976, 2012

PubMed Abstract: BtuCD is an ABC transporter catalyzing the uptake of vitamin B₁₂ across the Escherichia coli inner membrane. A previously reported X-ray structure of BtuCD in complex with the periplasmic vitamin B₁₂-binding protein BtuF revealed asymmetry of the transmembrane BtuC subunits. The functional relevance of this asymmetry has remained uncertain. Here we report the X-ray structure of a catalytically impaired BtuCD mutant in complex with BtuF, where the BtuC subunits adopt a distinct asymmetric conformation. The structure suggests that BtuF does not discriminate between, or impose, asymmetric conformations of BtuCD. It also explains the conformational disorder observed in BtuCDF crystals.

PubMed: 22569249
DOI: 10.1016/j.febslet.2012.02.042

Experimental method

X-RAY DIFFRACTION (3.493 Å)