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TitleConformational Change of a Tryptophan Residue in BtuF Facilitates Binding and Transport of Cobinamide by the Vitamin B12 Transporter BtuCD-F.
Journal, issue, pagesSci Rep, Vol. 7, Page 41575-41575, Year 2017
Publish dateOct 12, 2016 (structure data deposition date)
AuthorsMireku, S.A. / Ruetz, M. / Zhou, T. / Korkhov, V.M. / Krautler, B. / Locher, K.P.
External linksSci Rep / PubMed:28128319
MethodsX-ray diffraction
Resolution1.5 - 1.7 Å
Structure data

PDB-5m29:
Structure of cobinamide-bound BtuF, the periplasmic vitamin B12 binding protein in E.coli
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-5m2q:
Structure of cobinamide-bound BtuF mutant W66F, the periplasmic vitamin B12 binding protein in E.coli
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5m34:
Structure of cobinamide-bound BtuF mutant W66Y, the periplasmic vitamin B12 binding protein in E.coli
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5m3b:
Structure of cobinamide-bound BtuF mutant W66L, the periplasmic vitamin B12 binding protein in E.coli
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-CBY:
COB(II)INAMIDE

ChemComp-CYN:
CYANIDE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / BtuF / Cobinamide / periplasmic binding protein / ABC transporter

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