From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:2scp.jpg|left|200px]] | + | {{Seed}} |
| + | [[Image:2scp.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_2scp| PDB=2scp | SCENE= }} | | {{STRUCTURE_2scp| PDB=2scp | SCENE= }} |
| | | |
- | '''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_1560459}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 1560459 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_1560459}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 25: |
Line 29: |
| [[Category: Vijay-Kumar, S.]] | | [[Category: Vijay-Kumar, S.]] |
| [[Category: Binding protein]] | | [[Category: Binding protein]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:17:38 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:28:15 2008'' |
Revision as of 09:28, 29 July 2008
Template:STRUCTURE 2scp
STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 1560459
About this Structure
2SCP is a Single protein structure of sequence from Neanthes diversicolor. 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
Page seeded by OCA on Tue Jul 29 12:28:15 2008