Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
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Date
2012-04-05
Publication Type
Journal Article
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Abstract
BtuCD is an ABC transporter catalyzing the uptake of vitamin B12 across the Escherichia coli innermembrane. A previously reported X-ray structure of BtuCD in complex with the periplasmic vitaminB 12-binding protein BtuF revealed asymmetry of the transmembrane BtuC subunits. The functionalrelevance of this asymmetry has remained uncertain. Here we report the X-ray structure of a cata-lytically impaired BtuCD mutant in complex with BtuF, where the BtuC subunits adopt a distinctasymmetric conformation. The structure suggests that BtuF does not discriminate between, orimpose, asymmetric conformations of BtuCD. It also explains the conformational disorder observedin BtuCDF crystals.
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published
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Journal / series
Volume
586 (7)
Pages / Article No.
972 - 976
Publisher
Elsevier
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Date collected
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Subject
Membrane protein; ABC transporter; BtuCDF; Periplasmic binding protein; Asymmetry; X-ray structure
Organisational unit
03652 - Locher, Kaspar / Locher, Kaspar
09529 - Korkhov, Volodymyr / Korkhov, Volodymyr
Notes
Short communication.