3B9R
SERCA Ca2+-ATPase E2 aluminium fluoride complex without thapsigargin
3B9R の概要
| エントリーDOI | 10.2210/pdb3b9r/pdb |
| 分子名称 | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, TETRAFLUOROALUMINATE ION, MAGNESIUM ION, ... (6 entities in total) |
| 機能のキーワード | calcium pump, membrane protein, transition state, aluminium fluoride, dephosphorylation, alternative splicing, atp-binding, calcium, calcium transport, endoplasmic reticulum, hydrolase, ion transport, magnesium, metal-binding, nucleotide-binding, phosphorylation, sarcoplasmic reticulum, transmembrane, transport |
| 由来する生物種 | Oryctolagus cuniculus (rabbit) |
| 細胞内の位置 | Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 220548.33 |
| 構造登録者 | Olesen, C.,Picard, M.,Winther, A.M.L.,Morth, J.P.,Moller, J.V.,Nissen, P. (登録日: 2007-11-06, 公開日: 2007-12-18, 最終更新日: 2024-11-13) |
| 主引用文献 | Olesen, C.,Picard, M.,Winther, A.M.L.,Gyrup, C.,Morth, J.P.,Oxvig, C.,Moller, J.V.,Nissen, P. The structural basis of calcium transport by the calcium pump Nature, 450:1036-1042, 2007 Cited by PubMed Abstract: The sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase, representing the phosphoenzyme intermediates associated with Ca2+ binding, Ca2+ translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively. The structures complete the cycle of nucleotide binding and cation transport of Ca2+-ATPase. Phosphorylation of the enzyme triggers the onset of a conformational change that leads to the opening of a luminal exit pathway defined by the transmembrane segments M1 through M6, which represent the canonical membrane domain of P-type pumps. Ca2+ release is promoted by translocation of the M4 helix, exposing Glu 309, Glu 771 and Asn 796 to the lumen. The mechanism explains how P-type ATPases are able to form the steep electrochemical gradients required for key functions in eukaryotic cells. PubMed: 18075584DOI: 10.1038/nature06418 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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