4DBL

Crystal structure of E159Q mutant of BtuCDF

4DBL の概要

• エントリーDOI: 10.2210/pdb4dbl/pdb
• 分子名称: Vitamin B12 import system permease protein BtuC, Vitamin B12 import ATP-binding protein BtuD, Vitamin B12-binding protein, ... (5 entities in total)
• 機能のキーワード: abc transporter for vitamin b12, atp binding, inner membrane, transport protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P06609; Cell inner membrane; Peripheral membrane protein: P06611; Periplasm: P37028
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 316999.84

構造登録者

Korkhov, V.M.,Mireku, S.M.,Hvorup, R.N.,Locher, K.P. (登録日: 2012-01-16, 公開日: 2012-03-07, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.493 Å)