3trp

Crystal structure of recombinant rabbit skeletal calsequestrin

spinqualitylabelsall models 3trp, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3trp is a 1 chain structure with sequence from European rabbit. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MPD, MRD, NA Related: 3trq Gene: CASQ1 (European rabbit) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CASQ1_RABIT] Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca(2+) ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca(2+) ions (By similarity). Publication Abstract from PubMed Calsequestrin, the major calcium-storage protein of both cardiac and skeletal muscle, binds large amounts of Ca2+ in the sarcoplasmic reticulum and releases them during muscle contraction. For the first time, crystal structures of Ca2+-complexes for both human (hCASQ1) and rabbit skeletal calsequestrin (rCASQ1) were determined, clearly defining its Ca2+-sequestration capabilities through resolution of high- and low-affinity Ca2+-binding sites. rCASQ1 crystallized in low CaCl2 buffer revealed three high-affinity Ca2+ sites with trigonal bipyramidal, octahedral, and pentagonal bipyramidal coordination geometries, along with three low-affinity Ca2+ sites. hCASQ1 crystallized in high CaCl2 showed fifteen Ca2+ ions, which included the six Ca2+ ions in rCASQ1. Most of the low-affinity sites, some of which were mu-carboxylate-bridged, were established by the rotation of dimeric interfaces, indicating cooperative Ca2+-binding that is consistent with our atomic absorption spectroscopic data. Based on these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca2+-binding activity of calsequestrin. High-capacity Ca2+-binding of human skeletal calsequestrin.,Sanchez EJ, Lewis KM, Danna BR, Kang C J Biol Chem. 2012 Feb 15. PMID:22337878 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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