1T5T
Structure of the (SR)Ca2+-ATPase Ca2-E1-ADP:AlF4- form
Summary for 1T5T
| Entry DOI | 10.2210/pdb1t5t/pdb |
| Related | 1T5S |
| Descriptor | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 isoform SERCA1A, TETRAFLUOROALUMINATE ION, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | calcium pump, membrane protein, transition state, catalytic mechanism, phosphorylation, occlusion, hydrolase |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191 |
| Total number of polymer chains | 1 |
| Total formula weight | 110300.62 |
| Authors | Sorensen, T.L.-M.,Moller, J.V.,Nissen, P. (deposition date: 2004-05-05, release date: 2004-06-15, Last modification date: 2024-02-14) |
| Primary citation | Sorensen, T.L.,Moller, J.V.,Nissen, P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science, 304:1672-1675, 2004 Cited by PubMed Abstract: A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane. PubMed: 15192230DOI: 10.1126/science.1099366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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