2scp
From Proteopedia
(New page: 200px<br /><applet load="2scp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2scp, resolution 2.0Å" /> '''STRUCTURE OF A SARCOP...) |
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| - | [[Image:2scp.jpg|left|200px]]<br /><applet load="2scp" size=" | + | [[Image:2scp.jpg|left|200px]]<br /><applet load="2scp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2scp, resolution 2.0Å" /> | caption="2scp, resolution 2.0Å" /> | ||
'''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a sarcoplasmic Ca(2+)-binding protein (SCP) from | + | 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== | ==About this Structure== | ||
| - | 2SCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neanthes_diversicolor Neanthes diversicolor] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2SCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neanthes_diversicolor Neanthes diversicolor] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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== | ==Reference== | ||
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[[Category: Neanthes diversicolor]] | [[Category: Neanthes diversicolor]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cook, W | + | [[Category: Cook, W J.]] |
[[Category: Vijay-Kumar, S.]] | [[Category: Vijay-Kumar, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: binding protein]] | [[Category: binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:02 2008'' |
Revision as of 16:49, 21 February 2008
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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 Neanthes diversicolor with as ligand. This structure supersedes the now removed PDB entry 1SCP. Full crystallographic information is available from 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:1560459
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