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Structure paper

TitleDetermination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
Journal, issue, pagesMol. Microbiol., Vol. 79, Page 1515-1528, Year 2011
Publish dateJan 8, 2011 (structure data deposition date)
AuthorsWu, W. / Park, K.T. / Holyoak, T. / Lutkenhaus, J.
External linksMol. Microbiol. / PubMed:21231967
MethodsX-ray diffraction
Resolution2.343 Å
Structure data

PDB-3q9l:
The structure of the dimeric E.coli MinD-ATP complex
Method: X-RAY DIFFRACTION / Resolution: 2.343 Å

Chemicals

ChemComp-MG:
Unknown entry

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

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCELL CYCLE / HYDROLASE / ATPase / bacterial cell division inhibitor / MinC / MinE

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