1A8Y

CRYSTAL STRUCTURE OF CALSEQUESTRIN FROM RABBIT SKELETAL MUSCLE SARCOPLASMIC RETICULUM AT 2.4 A RESOLUTION

1A8Y の概要

• エントリーDOI: 10.2210/pdb1a8y/pdb
• 分子名称: CALSEQUESTRIN (2 entities in total)
• 機能のキーワード: calsequestrin, calcium-binding protein, sarcoplasmic reticulum, rabbit skeletal muscle
• 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: 42468.17

構造登録者

Wang, S.,Trumble, W.R.,Liao, H.,Wesson, C.R.,Dunker, A.K.,Kang, C. (登録日: 1998-03-31, 公開日: 1999-03-30, 最終更新日: 2024-02-07)

主引用文献

Wang, S.,Trumble, W.R.,Liao, H.,Wesson, C.R.,Dunker, A.K.,Kang, C.H.
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.
Nat.Struct.Biol., 5:476-483, 1998

PubMed Abstract: Calsequestrin, the major Ca2+ storage protein of muscle, coordinately binds and releases 40-50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. We have determined the structure of rabbit skeletal muscle calsequestrin. Three very negative thioredoxin-like domains surround a hydrophilic center. Each monomer makes two extensive dimerization contacts, both of which involve the approach of many negative groups. This structure suggests a mechanism by which calsequestrin may achieve high capacity Ca2+ binding. The suggested mechanism involves Ca2+-induced collapse of the three domains and polymerization of calsequestrin monomers arising from three factors: N-terminal arm exchange, helix-helix contacts and Ca2+ cross bridges. This proposed structure-based mechanism accounts for the observed coupling of high capacity Ca2+ binding with protein precipitation.

PubMed: 9628486
DOI: 10.1038/nsb0698-476

実験手法

X-RAY DIFFRACTION (2.4 Å)