2RPW
Structure of a peptide derived from H+-V-ATPase subunit a
Summary for 2RPW
| Entry DOI | 10.2210/pdb2rpw/pdb |
| Descriptor | 25 meric peptide from V-type proton ATPase subunit a, vacuolar isoform (1 entity in total) |
| Functional Keywords | v-atpase subunit a, acetylation, coiled coil, glycoprotein, hydrogen ion transport, ion transport, membrane, phosphoprotein, transmembrane, transport, vacuole, transport protein |
| Cellular location | Vacuole membrane ; Multi-pass membrane protein : P32563 |
| Total number of polymer chains | 1 |
| Total formula weight | 2832.33 |
| Authors | Vermeer, L.S.,Reat, V.,Hemminga, M.A.,Milon, A. (deposition date: 2008-11-08, release date: 2009-03-24, Last modification date: 2024-05-29) |
| Primary citation | Vermeer, L.S.,Reat, V.,Hemminga, M.A.,Milon, A. Structural properties of a peptide derived from H(+)-V-ATPase subunit a Biochim.Biophys.Acta, 1788:1204-1212, 2009 Cited by PubMed Abstract: The 3D structure of a peptide derived from the putative transmembrane segment 7 (TM7) of subunit a from H(+)-V-ATPase from Saccharomyces cerevisiae has been determined by solution state NMR in SDS. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738, as was previously suggested based on NMR studies of a similar peptide in DMSO. The pKa of both histidine residues that are important for proton transport was measured in water and in SDS. The differences that are found demonstrate that the histidine residues interact with the SDS polar heads. In detergent, circular dichroism data indicate that the secondary structure of the peptide depends on the pH and the type of detergent used. Using solid-state NMR, it is shown that the peptide is immobile in phospholipid bilayers, which means that it is probably not a single transmembrane helix in these samples. The environment is important for the structure of TM7, so in subunit a it is probably held in place by the other transmembrane helices of this subunit. PubMed: 19249284DOI: 10.1016/j.bbamem.2009.02.015 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
