6HH0
Yeast V-ATPase transmembrane helix 7 NMR structure in DPC micelles
Summary for 6HH0
| Entry DOI | 10.2210/pdb6hh0/pdb |
| NMR Information | BMRB: 34309 |
| Descriptor | V-type proton ATPase subunit a, vacuolar isoform (1 entity in total) |
| Functional Keywords | atpasse, transmembrane helix, dpc micelle, nmr spectroscopy, membrane protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 2832.33 |
| Authors | Zangger, K.,Hohlweg, W.,Wagner, G. (deposition date: 2018-08-24, release date: 2018-09-12, Last modification date: 2023-06-14) |
| Primary citation | Hohlweg, W.,Wagner, G.E.,Hofbauer, H.F.,Sarkleti, F.,Setz, M.,Gubensak, N.,Lichtenegger, S.,Falsone, S.F.,Wolinski, H.,Kosol, S.,Oostenbrink, C.,Kohlwein, S.D.,Zangger, K. A cation-pi interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment. J. Biol. Chem., 293:18977-18988, 2018 Cited by PubMed: 30209131DOI: 10.1074/jbc.RA118.005276 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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