3RRK
Crystal structure of the cytoplasmic N-terminal domain of subunit I, homolog of subunit a, of V-ATPase
Summary for 3RRK
| Entry DOI | 10.2210/pdb3rrk/pdb |
| Descriptor | V-type ATPase 116 kDa subunit, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | alpha beta fold, proton pump, subunit i/a, v-atpase, proton transport |
| Biological source | Meiothermus ruber |
| Total number of polymer chains | 1 |
| Total formula weight | 39410.98 |
| Authors | Srinivasan, S.,Vyas, N.K.,Baker, M.L.,Quiocho, F.A. (deposition date: 2011-04-29, release date: 2011-08-10, Last modification date: 2024-04-03) |
| Primary citation | Srinivasan, S.,Vyas, N.K.,Baker, M.L.,Quiocho, F.A. Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase. J.Mol.Biol., 412:14-21, 2011 Cited by PubMed Abstract: Subunit "a" is associated with the membrane-bound (V(O)) complex of eukaryotic vacuolar H(+)-ATPase acidification machinery. It has also been shown recently to be involved in diverse membrane fusion/secretory functions independent of acidification. Here, we report the crystal structure of the N-terminal cytosolic domain from the Meiothermus ruber subunit "I" homolog of subunit a. The structure is composed of a curved long central α-helix bundle capped on both ends by two lobes with similar α/β architecture. Based on the structure, a reasonable model of its eukaryotic subunit a counterpart was obtained. The crystal structure and model fit well into reconstructions from electron microscopy of prokaryotic and eukaryotic vacuolar H(+)-ATPases, respectively, clarifying their orientations and interactions and revealing features that could enable subunit a to play a role in membrane fusion/secretion. PubMed: 21787787DOI: 10.1016/j.jmb.2011.07.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.64 Å) |
Structure validation
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