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-Structure paper
Title | Rotation mechanism of Enterococcus hirae V(1)-ATPase based on asymmetric crystal structures |
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Journal, issue, pages | Nature, Vol. 493, Page 703-707, Year 2013 |
Publish date | Apr 3, 2012 (structure data deposition date) |
Authors | Arai, S. / Saijo, S. / Suzuki, K. / Mizutani, K. / Kakinuma, Y. / Ishizuka-Katsura, Y. / Ohsawa, N. / Terada, T. / Shirouzu, M. / Yokoyama, S. ...Arai, S. / Saijo, S. / Suzuki, K. / Mizutani, K. / Kakinuma, Y. / Ishizuka-Katsura, Y. / Ohsawa, N. / Terada, T. / Shirouzu, M. / Yokoyama, S. / Iwata, S. / Yamato, I. / Murata, T. |
External links | Nature / PubMed:23334411 |
Methods | X-ray diffraction |
Resolution | 2.172 - 3.9 Å |
Structure data | PDB-3vr2: PDB-3vr3: PDB-3vr4: PDB-3vr5: PDB-3vr6: |
Chemicals | ChemComp-HOH: ChemComp-ANP: ChemComp-MG: ChemComp-GOL: ChemComp-CL: ChemComp-B3P: |
Source |
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Keywords | HYDROLASE / V-ATPase / Enterococcus hirae / Rotary motor / P-loop / Na(+)-ATPase / ATP Binding |