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New page: left|200px<br /><applet load="2sas" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sas, resolution 2.4Å" /> '''STRUCTURE OF A SARCOP...
 
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[[Image:2sas.jpg|left|200px]]<br /><applet load="2sas" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2sas.jpg|left|200px]]<br /><applet load="2sas" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2sas, resolution 2.4&Aring;" />
caption="2sas, resolution 2.4&Aring;" />
'''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
2SAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2SAS OCA].  
2SAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SAS OCA].  


==Reference==
==Reference==
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[[Category: Branchiostoma lanceolatum]]
[[Category: Branchiostoma lanceolatum]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Babu, Y.S.]]
[[Category: Babu, Y S.]]
[[Category: Cook, W.J.]]
[[Category: Cook, W J.]]
[[Category: Cox, J.A.]]
[[Category: Cox, J A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]


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