1A8Y

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.

Wang, S.Trumble, W.R.Liao, H.Wesson, C.R.Dunker, A.K.Kang, C.H.

(1998) Nat Struct Biol 5: 476-483

  • DOI: https://doi.org/10.1038/nsb0698-476
  • Primary Citation of Related Structures:  
    1A8Y

  • 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.


  • Organizational Affiliation

    Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CALSEQUESTRIN367Oryctolagus cuniculusMutation(s): 0 
UniProt
Find proteins for P07221 (Oryctolagus cuniculus)
Explore P07221 
Go to UniProtKB:  P07221
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07221
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.188 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.74α = 90
b = 145.56β = 90
c = 111.79γ = 90
Software Package:
Software NamePurpose
PHASEmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-03-30
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Other