1rro: Difference between revisions

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OCA

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 <StructureSection load='1rro' size='340' side='right'caption='[[1rro]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RRO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rro]] is a 1 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=1RRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RRO FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#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=1rro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rro OCA], [https://pdbe.org/1rro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rro RCSB], [https://www.ebi.ac.uk/pdbsum/1rro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rro ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ONCO_RAT ONCO_RAT]] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
+[https://www.uniprot.org/uniprot/ONCO_RAT ONCO_RAT] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1rro ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-A refinement of the oncomodulin crystal structure at 1.30 A resolution has been carried out with X-ray data from the recombinant protein. The crystallographic R-factor values are 0.169 for 19,995 reflections in the range 6.0 to 1.30 A, which were used for the restrained least-squares refinement, and 0.176 for 20,186 observed reflections in the range 10.0 to 1.30 A. This high resolution refinement has enabled us to make more definitive statements about the molecular structure than was possible heretofore. The present model includes residues 1 to 108, the two Ca2+ of the CD and EF loops, two intermolecular Ca2+, and 103 water molecules per oncomodulin molecule. The electron density maps indicate disordered orientations for ten residues on the hydrophilic surface of the molecule. The pattern of molecular aggregation via intermolecular Ca2+, which occurs in the native rat oncomodulin structure, is also present in the recombinant oncomodulin structure. The Cys18 side-chain is not in a position that would be easily accessible for molecular dimerization via a disulphide bond. The substitution of Glu59, which is preserved in all the determined species of parvalbumin, by Asp59 in oncomodulin seems to break a stabilizing hydrogen bond in the CD loop and render the main-chain in positions 59 to 60 somewhat unstable. This instability in the CD loop, and the strong tendency of oncomodulin for molecular aggregation via intermolecular Ca2+, appear to be the two outstanding features that may account for oncomodulin's biological peculiarities.
-Refinement of recombinant oncomodulin at 1.30 A resolution.,Ahmed FR, Rose DR, Evans SV, Pippy ME, To R J Mol Biol. 1993 Apr 20;230(4):1216-24. PMID:8487302<ref>PMID:8487302</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1rro" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Parvalbumin|Parvalbumin]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Black rat]]
 [[Category: Large Structures]]
-[[Category: Ahmed, F R]]
+[[Category: Rattus rattus]]
-[[Category: Evans, S V]]
+[[Category: Ahmed FR]]
-[[Category: Pippy, M E]]
+[[Category: Evans SV]]
-[[Category: Rose, D R]]
+[[Category: Pippy ME]]
-[[Category: To, R]]
+[[Category: Rose DR]]
-[[Category: Calcium-binding protein]]
+[[Category: To R]]