2sas
From Proteopedia
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| - | [[Image:2sas.jpg|left|200px]] | + | [[Image:2sas.jpg|left|200px]] |
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| - | '''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2sas |SIZE=350|CAPTION= <scene name='initialview01'>2sas</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SAS is a [ | + | 2SAS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SAS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8429557 8429557] |
[[Category: Branchiostoma lanceolatum]] | [[Category: Branchiostoma lanceolatum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:13 2008'' |
Revision as of 16:38, 20 March 2008
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| , resolution 2.4Å | |||||||
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| 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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