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-Structure paper
Title | Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases. |
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Journal, issue, pages | Embo Rep., Vol. 25, Page 853-875, Year 2024 |
Publish date | Sep 12, 2022 (structure data deposition date) |
Authors | Strauss, J. / Wilkinson, C. / Vidilaseris, K. / de Castro Ribeiro, O.M. / Liu, J. / Hillier, J. / Wichert, M. / Malinen, A.M. / Gehl, B. / Jeuken, L.J. ...Strauss, J. / Wilkinson, C. / Vidilaseris, K. / de Castro Ribeiro, O.M. / Liu, J. / Hillier, J. / Wichert, M. / Malinen, A.M. / Gehl, B. / Jeuken, L.J. / Pearson, A.R. / Goldman, A. |
External links | Embo Rep. / PubMed:38182815 |
Methods | X-ray diffraction |
Resolution | 2.59 - 4.53 Å |
Structure data | PDB-8b21: PDB-8b22: PDB-8b23: PDB-8b24: PDB-8b37: |
Chemicals | ChemComp-LMT: ChemComp-PEG: ChemComp-PGE: ChemComp-PG4: ChemComp-HOH: ChemComp-DPO: ChemComp-MG: ChemComp-K: ChemComp-PO4: ChemComp-2PN: ChemComp-SO4: |
Source |
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Keywords | MEMBRANE PROTEIN / Membrane bound pyrophosphatase / enzyme / complex / K+-independence / Ion-selectivity / Membrane Proteins / Membrane-bound pyrophosphatases. |