5kn1 | pdb_00005kn1

Recombinant bovine skeletal calsequestrin, high-Ca2+ form

spinqualitylabelsall models 5kn1, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kn1 is a 3 chain structure with sequence from Bos taurus. This structure supersedes the now removed PDB entry 4tly. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.137Å Ligands: CA, CL, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q05JF3_BOVIN Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle.[RuleBase:RU000648] Publication Abstract from PubMed Calsequestrin is glycosylated and phosphorylated during its transit to its final destination in the junctional sarcoplasmic reticulum. To determine the significance and universal profile of these post-translational modifications to mammalian calsequestrin, we characterized, via mass spectrometry, the glycosylation and phosphorylation of skeletal muscle calsequestrin from cattle (B. taurus), lab mice (M. musculus) and lab rats (R. norvegicus) and cardiac muscle calsequestrin from cattle, lab rats and humans. On average, glycosylation of skeletal calsequestrin consisted of two N-acetylglucosamines and one mannose (GlcNAc(2)Man(1)), while cardiac calsequestrin had five additional mannoses (GlcNAc(2)Man(6)). Skeletal calsequestrin was not phosphorylated, while the C-terminal tails of cardiac calsequestrin contained between zero to two phosphoryls, indicating that phosphorylation of cardiac calsequestrin may be heterogeneous in vivo. Static light scattering experiments showed that the Ca(2+)-dependent polymerization capabilities of native bovine skeletal calsequestrin are enhanced, relative to the non-glycosylated, recombinant isoform, which our crystallographic studies suggest may be due to glycosylation providing a dynamic "guiderail"-like scaffold for calsequestrin polymerization. Glycosylation likely increases a polymerization/depolymerization response to changing Ca(2+) concentrations, and proper glycosylation, in turn, guarantees both effective Ca(2+) storage/buffering of the sarcoplasmic reticulum and localization of calsequestrin (Casq) at its target site. Characterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle.,Lewis KM, Munske GR, Byrd SS, Kang J, Cho HJ, Rios E, Kang C Int J Mol Sci. 2016 Sep 13;17(9). pii: E1539. doi: 10.3390/ijms17091539. PMID:27649144 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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