Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF

FEBS Letters
Vladimir M KorkhovKaspar P Locher

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.

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Citations

May 10, 2013·The Journal of Biological Chemistry·Po-Chao WenEmad Tajkhorshid
Nov 18, 2014·Nature Structural & Molecular Biology·Vladimir M KorkhovKaspar P Locher
Mar 19, 2014·The Journal of General Physiology·Josy ter BeekDirk Jan Slotboom
Mar 22, 2014·Progress in Biophysics and Molecular Biology·Gábor Maksay, Orsolya Tőke
Oct 26, 2013·Trends in Microbiology·Peng Zhang
Aug 27, 2014·Critical Reviews in Biochemistry and Molecular Biology·Austin J RiceHeather W Pinkett
Nov 11, 2016·Nature Communications·Youichi NaoeHiroshi Sugimoto
Mar 4, 2017·Molecular Microbiology·Laura TeichmannErhard Bremer
Jan 21, 2017·Journal of Molecular Biology·Oded Lewinson, Nurit Livnat-Levanon
Sep 25, 2012·Nature·Vladimir M KorkhovKaspar P Locher
Feb 4, 2021·MBio·Zhenyao LuoChristopher A McDevitt
Nov 10, 2018·ACS Central Science·Marten PrießLars V Schäfer

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