1VFP
Crystal structure of the SR CA2+-ATPase with bound AMPPCP
Summary for 1VFP
| Entry DOI | 10.2210/pdb1vfp/pdb |
| Related | 1IWO 1SU4 |
| Descriptor | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | membrane protein, p-type atpase, had fold, hydrolase |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191 |
| Total number of polymer chains | 2 |
| Total formula weight | 220424.49 |
| Authors | Toyoshima, C.,Mizutani, T. (deposition date: 2004-04-18, release date: 2004-07-06, Last modification date: 2024-11-20) |
| Primary citation | Toyoshima, C.,Mizutani, T. Crystal structure of the calcium pump with a bound ATP analogue. Nature, 430:529-535, 2004 Cited by PubMed Abstract: P-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across cell and organelle membranes. Here, we describe the crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic reticulum, a representative member of the P-type ATPase superfamily, with an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites. In this state, the ATP analogue reorganizes the three cytoplasmic domains (A, N and P), which are widely separated without nucleotide, by directly bridging the N and P domains. The structure of the P-domain itself is altered by the binding of the ATP analogue and Mg2+. As a result, the A-domain is tilted so that one of the transmembrane helices moves to lock the cytoplasmic gate of the transmembrane Ca2+-binding sites. This appears to be the mechanism for occluding the bound Ca2+ ions, before releasing them into the lumen of the sarcoplasmic reticulum. PubMed: 15229613DOI: 10.1038/nature02680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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