2sas

STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION

spinqualitylabelsall models 2sas, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2sas is a 1 chain structure with sequence from Amphioxus lanceolatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SCP2_BRALA] Like parvalbumins, SCP's seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of a sarcoplasmic Ca(2+)-binding protein from the protochordate amphioxus has been determined at 2.4 A resolution using multiple-isomorphous-replacement techniques. The refined model includes all 185 residues, three calcium ions, and one water molecule. The final crystallographic R-factor is 0.199. Bond lengths and bond angles in the molecules have root-mean-square deviations from ideal values of 0.015 A and 2.8 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core, unlike the extended dumbbell-shaped structures of calmodulin or troponin C. There are four distinct domains with the typical helix-loop-helix Ca(2+)-binding motif (EF hand). The conformation of the pair of EF hands in the N-terminal half of the protein is unusual due to the presence of an aspartate residue in the twelfth position of the first Ca(2+)-binding loop, rather than the usual glutamate. The C-terminal half of the molecule contains one Ca(2+)-binding domain with a novel helix-loop-helix conformation and one Ca(2+)-binding domain that is no longer functional because of amino acid changes. The overall structure is quite similar to a sarcoplasmic Ca(2+)-binding protein from sandworm, although there is only about 12% amino acid sequence identity between them. The similarity of the structures of these two proteins suggests that all sarcoplasmic Ca(2+)-binding proteins will have the same general conformation, even though there is very little conservation of primary structure among the proteins from various species. Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 A resolution.,Cook WJ, Jeffrey LC, Cox JA, Vijay-Kumar S J Mol Biol. 1993 Jan 20;229(2):461-71. PMID:8429557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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