Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum

Shuren Wang, William R. Trumble, Hong Liao, Carla R. Wesson, A. Dunker, ChulHee Kang

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

Caisequestrin, 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 o 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.

Original languageEnglish (US)
Pages (from-to)476-483
Number of pages8
JournalNature Structural Biology
Volume5
Issue number6
DOIs
StatePublished - Jun 1998
Externally publishedYes

Fingerprint

Calsequestrin
Sarcoplasmic Reticulum
Muscle
Skeletal Muscle
Crystal structure
Rabbits
Monomers
Thioredoxins
Dimerization
Muscle Proteins
Polymerization
Carrier Proteins
Ions
Molecules
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. / Wang, Shuren; Trumble, William R.; Liao, Hong; Wesson, Carla R.; Dunker, A.; Kang, ChulHee.

In: Nature Structural Biology, Vol. 5, No. 6, 06.1998, p. 476-483.

Research output: Contribution to journalArticle

Wang, Shuren ; Trumble, William R. ; Liao, Hong ; Wesson, Carla R. ; Dunker, A. ; Kang, ChulHee. / Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. In: Nature Structural Biology. 1998 ; Vol. 5, No. 6. pp. 476-483.
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