4PGS
Crystal structure of YetJ from Bacillus Subtilis at pH 6 by soaking
Summary for 4PGS
| Entry DOI | 10.2210/pdb4pgs/pdb |
| Related | 4PGR 4PGU 4PGV 4PGW |
| Descriptor | Uncharacterized protein YetJ (2 entities in total) |
| Functional Keywords | membrane protein, 7-tms, triple-helix sandwich, di-aspartyl ph sensor, calcium leak, open-conformation, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, membrance protein |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Multi-pass membrane protein (Potential): O31539 |
| Total number of polymer chains | 1 |
| Total formula weight | 24116.81 |
| Authors | Liu, Q.,Chang, Y.,Hendrickson, W.A.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2014-05-02, release date: 2014-06-04, Last modification date: 2023-12-27) |
| Primary citation | Chang, Y.,Bruni, R.,Kloss, B.,Assur, Z.,Kloppmann, E.,Rost, B.,Hendrickson, W.A.,Liu, Q. Structural basis for a pH-sensitive calcium leak across membranes. Science, 344:1131-1135, 2014 Cited by PubMed Abstract: Calcium homeostasis balances passive calcium leak and active calcium uptake. Human Bax inhibitor-1 (hBI-1) is an antiapoptotic protein that mediates a calcium leak and is representative of a highly conserved and widely distributed family, the transmembrane Bax inhibitor motif (TMBIM) proteins. Here, we present crystal structures of a bacterial homolog and characterize its calcium leak activity. The structure has a seven-transmembrane-helix fold that features two triple-helix sandwiches wrapped around a central C-terminal helix. Structures obtained in closed and open conformations are reversibly interconvertible by change of pH. A hydrogen-bonded, pKa (where Ka is the acid dissociation constant)-perturbed pair of conserved aspartate residues explains the pH dependence of this transition, and biochemical studies show that pH regulates calcium influx in proteoliposomes. Homology models for hBI-1 provide insights into TMBIM-mediated calcium leak and cytoprotective activity. PubMed: 24904158DOI: 10.1126/science.1252043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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