2scp: Difference between revisions

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-[[Image:2scp.jpg|left|200px]]
- {{Structure
+==STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION==
-|PDB= 2scp |SIZE=350|CAPTION= <scene name='initialview01'>2scp</scene>, resolution 2.0&Aring;
+<StructureSection load='2scp' size='340' side='right'caption='[[2scp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
+<table><tr><td colspan='2'>[[2scp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hediste_diversicolor Hediste diversicolor]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1scp 1scp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2SCP FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2scp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2scp OCA], [https://pdbe.org/2scp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2scp RCSB], [https://www.ebi.ac.uk/pdbsum/2scp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2scp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SCP_HEDDI SCP_HEDDI] Like parvalbumins, SCP's seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/2scp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2scp ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 ANGSTROMS RESOLUTION'''
+==See Also==
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Hediste diversicolor]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Cook WJ]]
-SCP 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].
+[[Category: Vijay-Kumar S]]
-==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: CA]]
-[[Category: binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:13 2008''