1rtp: Difference between revisions

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-[[Image:1rtp.jpg|left|200px]]<br /><applet load="1rtp" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rtp, resolution 2.0&Aring;" />
-'''REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION'''<br />
-==Overview==
+==REFINED X-RAY STRUCTURE OF RAT PARVALBUMIN, A MAMMALIAN ALPHA-LINEAGE PARVALBUMIN, AT 2.0 A RESOLUTION==
-We present here the X-ray crystal structure of the rat alpha-parvalbumin, from fast twitch muscle. This protein (M(r) 11.8 kDa) crystallizes in, space group P2(1)2(1)2(1) with unit cell dimensions of a = 34.3 A, b =, 55.0 A, c = 156.1 A and three molecules in the asymmetric unit. The, protein structure was solved by the molecular replacement method and has, been refined to a crystallographic R-factor [formula: see text] of 0.181, for all reflections with I/sigma(I) &gt; or = 2 (I = intensity) between 8.0, and 2.0 A resolution. The molecules located most easily in the molecular, replacement rotation function had lower overall thermal motion parameters, and higher numbers of intermolecular crystal packing contacts. The overall, fold of the polypeptide chain for the rat alpha-parvalbumin is similar to, other known parvalbumin structures (root-mean-square deviations in, alpha-carbon atom positions range from 0.60 to 0.87 A). There are two, Ca(2+)-binding sites in parvalbumins, and there is some evidence for a, third ion-binding site, adjacent to the CD site, in the rat species. The, level of structural variability among the best-ordered regions of the, three independent rat alpha-parvalbumin molecules in the crystallographic, asymmetric unit is two to three times higher than the mean coordinate, error (0.10 A), indicating flexibility in the molecule. Sequence, differences between alpha and beta-lineage parvalbumins result in, repacking of the hydrophobic core and some shifts in the protein backbone., The shifts are localized, however, and entire helices do not shift as, rigid units.
+<StructureSection load='1rtp' size='340' side='right'caption='[[1rtp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rtp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RTP FirstGlance]. <br>
+</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>
+<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=1rtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtp OCA], [https://pdbe.org/1rtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rtp RCSB], [https://www.ebi.ac.uk/pdbsum/1rtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rtp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRVA_RAT PRVA_RAT] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
+== 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/rt/1rtp_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=1rtp ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-RTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] 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=1RTP OCA].
+*[[Parvalbumin|Parvalbumin]]
+__TOC__
-==Reference==
+</StructureSection>
-Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0 A resolution., McPhalen CA, Sielecki AR, Santarsiero BD, James MN, J Mol Biol. 1994 Jan 14;235(2):718-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8289291 8289291]
+[[Category: Large Structures]]
 [[Category: Rattus rattus]]
-[[Category: Single protein]]
+[[Category: James MNG]]
-[[Category: James, M.N.G.]]
+[[Category: Mcphalen CA]]
-[[Category: Mcphalen, C.A.]]
+[[Category: Santarsiero BD]]
-[[Category: Santarsiero, B.D.]]
+[[Category: Sielecki AR]]
-[[Category: Sielecki, A.R.]]
-[[Category: CA]]
-[[Category: calcium-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:51:41 2007''