3TRP

Crystal structure of recombinant rabbit skeletal calsequestrin

3TRP の概要

• エントリーDOI: 10.2210/pdb3trp/pdb
• 関連するPDBエントリー: 3TRQ
• 分子名称: Calsequestrin-1, (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total)
• 機能のキーワード: calcium-binding protein
• 由来する生物種: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits)
• 細胞内の位置: Sarcoplasmic reticulum lumen: P07221
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41588.05

構造登録者

Sanchez, E.J.,Lewis, K.M.,Munske, G.R.,Nissen, M.S.,Kang, C. (登録日: 2011-09-09, 公開日: 2012-02-22, 最終更新日: 2023-09-13)

主引用文献

Sanchez, E.J.,Lewis, K.M.,Danna, B.R.,Kang, C.
High-capacity Ca2+ Binding of Human Skeletal Calsequestrin.
J.Biol.Chem., 287:11592-11601, 2012

PubMed Abstract: Calsequestrin, the major calcium storage protein in both cardiac and skeletal muscle, binds large amounts of Ca(2+) in the sarcoplasmic reticulum and releases them during muscle contraction. For the first time, the crystal structures of Ca(2+) complexes for both human (hCASQ1) and rabbit (rCASQ1) skeletal calsequestrin were determined, clearly defining their Ca(2+) sequestration capabilities through resolution of high- and low-affinity Ca(2+)-binding sites. rCASQ1 crystallized in low CaCl(2) buffer reveals three high-affinity Ca(2+) sites with trigonal bipyramidal, octahedral, and pentagonal bipyramidal coordination geometries, along with three low-affinity Ca(2+) sites. hCASQ1 crystallized in high CaCl(2) shows 15 Ca(2+) ions, including the six Ca(2+) ions in rCASQ1. Most of the low-affinity sites, some of which are μ-carboxylate-bridged, are established by the rotation of dimer interfaces, indicating cooperative Ca(2+) binding that is consistent with our atomic absorption spectroscopic data. On the basis of these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca(2+)-binding activity of calsequestrin.

PubMed: 22337878
DOI: 10.1074/jbc.M111.335075

実験手法

X-RAY DIFFRACTION (1.8817 Å)