5A3S

Crystal structure of the (SR) Calcium ATPase E2-vanadate complex bound to thapsigargin and TNP-ATP

5A3S の概要

• エントリーDOI: 10.2210/pdb5a3s/pdb
• 関連するPDBエントリー: 5A3Q 5A3R
• 分子名称: SARCOPLASMIC RETICULUM CALCIUM ATPASE 1 MOLECULE SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1, OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX Y]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER, oxido(dioxo)vanadium, ... (8 entities in total)
• 機能のキーワード: hydrolase, sarco(endo)plasmic reticulum calcium atpase, beryllium fluoride, p-type atpase, serca, trinitrophenyl-nucleotide analoges, tnp-atp, calcium transport, inhibition, transition state
• 由来する生物種: ORYCTOLAGUS CUNICULUS (RABBIT)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 222439.48

構造登録者

Clausen, J.D.,Bublitz, M.,Arnou, B.,Olesen, C.,Andersen, J.P.,Moller, J.V.,Nissen, P. (登録日: 2015-06-03, 公開日: 2016-04-13, 最終更新日: 2024-10-23)

主引用文献

Clausen, J.D.,Bublitz, M.,Arnou, B.,Olesen, C.,Andersen, J.P.,Moller, J.V.,Nissen, P.
Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase.
Structure, 24:617-, 2016

PubMed Abstract: Vanadate is the hallmark inhibitor of the P-type ATPase family; however, structural details of its inhibitory mechanism have remained unresolved. We have determined the crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase with bound vanadate in the absence of Ca(2+). Vanadate is bound at the catalytic site as a planar VO3(-) in complex with water and Mg(2+) in a dephosphorylation transition-state-like conformation. Validating bound VO3(-) by anomalous difference Fourier maps using long-wavelength data we also identify a hitherto undescribed Cl(-) site near the dephosphorylation site. Crystallization was facilitated by trinitrophenyl (TNP)-derivatized nucleotides that bind with the TNP moiety occupying the binding pocket that normally accommodates the adenine of ATP, rationalizing their remarkably high affinity for E2P-like conformations of the Ca(2+)-ATPase. A comparison of the configurations of bound nucleotide analogs in the E2·VO3(-) structure with that in E2·BeF3(-) (E2P ground state analog) reveals multiple binding modes to the Ca(2+)-ATPase.

PubMed: 27050689
DOI: 10.1016/J.STR.2016.02.018

実験手法

X-RAY DIFFRACTION (3.3 Å)