5ZMV

Crystal structure of the E309A mutant of SR Ca2+-ATPase in E2(TG)

5ZMV の概要

• エントリーDOI: 10.2210/pdb5zmv/pdb
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, SULFATE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, had fold, atp-binding, calcium transport, endoplasmic reticulum, ion transport, magnesium, metal-binding, nucleotide-binding, phosphorylation, sarcoplasmic reticulum, transmembrane, transport, hydrolase
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 113184.10

構造登録者

Ogawa, H.,Hirata, A.,Tsueda, J.,Toyoshima, C. (登録日: 2018-04-06, 公開日: 2018-12-12, 最終更新日: 2024-11-13)

主引用文献

Tsunekawa, N.,Ogawa, H.,Tsueda, J.,Akiba, T.,Toyoshima, C.
Mechanism of the E2 to E1 transition in Ca2+pump revealed by crystal structures of gating residue mutants.
Proc. Natl. Acad. Sci. U.S.A., 115:12722-12727, 2018

PubMed Abstract: Ca-ATPase of sarcoplasmic reticulum (SERCA1a) pumps two Ca per ATP hydrolyzed from the cytoplasm and two or three protons in the opposite direction. In the E2 state, after transferring Ca into the lumen of sarcoplasmic reticulum, all of the acidic residues that coordinate Ca are thought to be protonated, including the gating residue Glu309. Therefore a Glu309Gln substitution is not expected to significantly perturb the structure. Here we report crystal structures of the Glu309Gln and Glu309Ala mutants of SERCA1a under E2 conditions. The Glu309Gln mutant exhibits, unexpectedly, large structural rearrangements in both the cytoplasmic and transmembrane domains, apparently uncoupling them. However, the structure definitely represents E2 and, together with the help of quantum chemical calculations, allows us to postulate a mechanism for the E2 → E1 transition triggered by deprotonation of Glu309.

PubMed: 30482857
DOI: 10.1073/pnas.1815472115

実験手法

X-RAY DIFFRACTION (3.3 Å)