Asymmetric states of vitamin B 12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF

Korkhov, Vladimir M., Mireku, Samantha A., Hvorup, Rikki N. and Locher, Kaspar P. (2012) Asymmetric states of vitamin B 12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF. FEBS Letters, 586 7: 972-976. doi:10.1016/j.febslet.2012.02.042


Author Korkhov, Vladimir M.
Mireku, Samantha A.
Hvorup, Rikki N.
Locher, Kaspar P.
Title Asymmetric states of vitamin B 12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
Formatted title
Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
Journal name FEBS Letters   Check publisher's open access policy
ISSN 0014-5793
1873-3468
Publication date 2012-04-05
Sub-type Article (original research)
DOI 10.1016/j.febslet.2012.02.042
Open Access Status
Volume 586
Issue 7
Start page 972
End page 976
Total pages 5
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Formatted 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.
Keyword ABC transporter
Asymmetry
BtuCDF
Membrane protein
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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