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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) |
![]() | 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. |
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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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![]() | HYDROLASE / V-ATPase / Enterococcus hirae / Rotary motor / P-loop / Na(+)-ATPase / ATP Binding |