2NVJ
NMR structures of transmembrane segment from subunit a from the yeast proton V-ATPase
Summary for 2NVJ
| Entry DOI | 10.2210/pdb2nvj/pdb |
| NMR Information | BMRB: 15025 |
| Descriptor | 25mer peptide from Vacuolar ATP synthase subunit a, vacuolar isoform (1 entity in total) |
| Functional Keywords | alfa helix, 3, 10 helix, pi helix, hydrolase |
| Cellular location | Vacuole membrane; Multi-pass membrane protein: P32563 |
| Total number of polymer chains | 1 |
| Total formula weight | 2837.26 |
| Authors | Hemminga, M.A.,van Mierlo, C.P.,Wechselberger, R.,de Jong, E.R.,Duarte, A.M. (deposition date: 2006-11-13, release date: 2007-10-02, Last modification date: 2024-11-13) |
| Primary citation | Duarte, A.M.,de Jong, E.R.,Wechselberger, R.,van Mierlo, C.P.,Hemminga, M.A. Segment TM7 from the cytoplasmic hemi-channel from V(O)-H(+)-V-ATPase includes a flexible region that has a potential role in proton translocation Biochim.Biophys.Acta, 1768:2263-2270, 2007 Cited by PubMed Abstract: A 900-MHz NMR study is reported of peptide sMTM7 that mimics the cytoplasmic proton hemi-channel domain of the seventh transmembrane segment (TM7) from subunit a of H(+)-V-ATPase from Saccharomyces cerevisiae. The peptide encompasses the amino acid residues known to actively participate in proton translocation. In addition, peptide sMTM7 contains the amino acid residues that upon mutation cause V-ATPase to become resistant against the inhibitor bafilomycin. 2D TOCSY and NOESY (1)H-(1)H NMR spectra are obtained of sMTM7 dissolved in d(6)-DMSO and are used to calculate the three-dimensional structure of the peptide. The NMR-based structures and corresponding dynamical features of peptide sMTM7 show that sMTM7 is composed of two alpha-helical regions. These regions are separated by a flexible hinge of two residues. The hinge acts as a ball-and-joint socket and both helical segments move independently with respect to one another. This movement in TM7 is suggested to cause the opening and closing of the cytoplasmic proton hemi-channel and enables proton translocation. PubMed: 17573038DOI: 10.1016/j.bbamem.2007.05.014 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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