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Structure paper

TitleStudies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 11290-11296, Year 2010
Publish dateJun 4, 2009 (structure data deposition date)
AuthorsGould, A.D. / Shilton, B.H.
External linksJ. Biol. Chem. / PubMed:20147285
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-3hpi:
Crystal structure of maltose-binding protein mutant with bound sucrose
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3kjt:
Stimulation of the maltose transporter by a mutant sucrose binding protein gives insights into ABC transporter coupling
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsSUGAR BINDING PROTEIN / periplasmic binding protein / MBP / Sugar transport / Transport / TRANSPORT PROTEIN / Alternate conformation / Periplasm

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