4YCN

Crystal structure of the calcium pump with bound marine macrolide BLLB

4YCN の概要

• エントリーDOI: 10.2210/pdb4ycn/pdb
• 関連するPDBエントリー: 4YCM
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, SODIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, had fold, ca2+, ion pump, 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: 111756.42

構造登録者

Morita, M.,Ogawa, H.,Ohno, O.,Yamori, T.,Suenaga, K.,Toyoshima, C. (登録日: 2015-02-20, 公開日: 2016-01-13, 最終更新日: 2020-02-05)

主引用文献

Morita, M.,Ogawa, H.,Ohno, O.,Yamori, T.,Suenaga, K.,Toyoshima, C.
Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding
Febs Lett., 589:1406-1411, 2015

PubMed Abstract: Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (Ki∼10 nM) inhibitors of Ca(2+)-pumps with a unique binding mode. The crystal structures of the Ca(2+)-pump in complex with BLSs at 3.2-3.5 Å-resolution show that BLSs bind to the pump near the cytoplasmic surface of the transmembrane region. The crystal structures and activity measurement of BLS analogs allow us to identify the structural features that confer high potency to BLSs as inhibitors of the pump.

PubMed: 25957767
DOI: 10.1016/j.febslet.2015.04.056

実験手法

X-RAY DIFFRACTION (3.5 Å)