View source for 2scp

[[Image:2scp.jpg|left|200px]]

 {{Structure
|PDB= 2scp |SIZE=350|CAPTION= <scene name='initialview01'>2scp</scene>, resolution 2.0&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY= 
|GENE= 
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2scp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2scp OCA], [http://www.ebi.ac.uk/pdbsum/2scp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2scp RCSB]</span>
}}

'''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION'''


==Overview==
The crystal structure of a sarcoplasmic Ca(2+)-binding protein (SCP) from the sandworm Nereis diversicolor has been determined and refined at 2.0 A resolution using restrained least-squares techniques. The two molecules in the crystallographic asymmetric unit, which are related by a non-crystallographic 2-fold axis, were refined independently. The refined model includes all 174 residues and three calcium ions for each molecule, as well as 213 water molecules. The root-mean-square difference in co-ordinates for backbone atoms and calcium ions of the two molecules is 0.51 A. The final crystallographic R-factor, based on 18,959 reflections in the range 2.0 A less than or equal to d less than or equal to 7.0 A, with intensities exceeding 2.0 sigma, is 0.182. Bond lengths and bond angles in the molecules have root-mean-square deviations from ideal values of 0.013 A and 2.2 degrees, respectively. SCP has four distinct domains with the typical helix-loop-helix (EF-hand) Ca(2+)-binding motif, although the second Ca(2+)-binding domain is not functional due to amino acid changes in the loop. The structure shows several unique features compared to other Ca(2+)-binding proteins with four EF-hand domains. The overall structure is highly compact and globular with a predominant hydrophobic core, unlike the extended dumbbell-shaped structure of calmodulin or troponin C. A hydrophobic tail at the COOH terminus adds to the structural stability by packing against a hydrophobic pocket created by the folding of the NH2 and COOH-terminal Ca(2+)-binding domain pairs. The first and second domains show different helix-packing arrangements from any previously described for Ca(2+)-binding proteins.

==About this Structure==
2SCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neanthes_diversicolor Neanthes diversicolor]. This structure supersedes the now removed PDB entry 1SCP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SCP OCA]. 

==Reference==
Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 A resolution., Vijay-Kumar S, Cook WJ, J Mol Biol. 1992 Mar 20;224(2):413-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1560459 1560459]
[[Category: Neanthes diversicolor]]
[[Category: Single protein]]
[[Category: Cook, W J.]]
[[Category: Vijay-Kumar, S.]]
[[Category: binding protein]]

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