6LY8
V/A-ATPase from Thermus thermophilus, the soluble domain, including V1, d, two EG stalks, and N-terminal domain of a-subunit.
Summary for 6LY8
Entry DOI | 10.2210/pdb6ly8/pdb |
EMDB information | 30014 |
Descriptor | V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (5 entities in total) |
Functional Keywords | rotary atpase, v/a-atpase, molecular motor, motor protein |
Biological source | Thermus thermophilus HB8 More |
Total number of polymer chains | 8 |
Total formula weight | 387196.11 |
Authors | Kishikawa, J.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. (deposition date: 2020-02-13, release date: 2020-09-09, Last modification date: 2020-09-30) |
Primary citation | Kishikawa, J.I.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. Mechanical inhibition of isolated V o from V/A-ATPase for proton conductance. Elife, 9:-, 2020 Cited by PubMed: 32639230DOI: 10.7554/eLife.56862 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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