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Structure paper

TitleDecoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 111, Page 4982-4987, Year 2014
Publish dateMar 5, 2014 (structure data deposition date)
AuthorsSherman, D.J. / Lazarus, M.B. / Murphy, L. / Liu, C. / Walker, S. / Ruiz, N. / Kahne, D.
External linksProc. Natl. Acad. Sci. USA / PubMed:24639492
MethodsX-ray diffraction
Resolution1.55 - 2.05 Å
Structure data

PDB-4p31:
Crystal structure of a selenomethionine derivative of E. coli LptB in complex with ADP-Magensium
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-4p32:
Crystal structure of E. coli LptB in complex with ADP-magnesium
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4p33:
Crystal structure of E. coli LptB-E163Q in complex with ATP-sodium
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / ABC transporter / nucleotide-binding domain / ATPase / ATP binding

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