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Structure paper

TitleThe Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 146, Page 396-407, Year 2011
Publish dateMar 25, 2011 (structure data deposition date)
AuthorsPark, K.T. / Wu, W. / Battaile, K.P. / Lovell, S. / Holyoak, T. / Lutkenhaus, J.
External linksCell(Cambridge,Mass. ) / PubMed:21816275
MethodsX-ray diffraction
Resolution2.6 - 4.3 Å
Structure data

PDB-3r9i:
2.6A resolution structure of MinD complexed with MinE (12-31) peptide
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3r9j:
4.3A resolution structure of a MinD-MinE(I24N) protein complex
Method: X-RAY DIFFRACTION / Resolution: 4.3 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsCELL CYCLE / HYDROLASE/CELL CYCLE / ATPase / bacterial cell division inhibitor / mine / HYDROLASE-CELL CYCLE complex / protein complex

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