2sas
From Proteopedia
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|PDB= 2sas |SIZE=350|CAPTION= <scene name='initialview01'>2sas</scene>, resolution 2.4Å | |PDB= 2sas |SIZE=350|CAPTION= <scene name='initialview01'>2sas</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sas OCA], [http://www.ebi.ac.uk/pdbsum/2sas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2sas RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Cook, W J.]] | [[Category: Cook, W J.]] | ||
[[Category: Cox, J A.]] | [[Category: Cox, J A.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:44 2008'' |
Revision as of 02:02, 31 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
2SAS is a Single protein structure of sequence from Branchiostoma lanceolatum. Full crystallographic information is available from OCA.
Reference
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
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