1rro

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[[Image:1rro.jpg|left|200px]]
 
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==REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1rro", creates the "Structure Box" on the page.
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<StructureSection load='1rro' size='340' side='right'caption='[[1rro]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1rro| PDB=1rro | SCENE= }}
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rr/1rro_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Parvalbumin|Parvalbumin]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Rattus rattus]]
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==About this Structure==
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[[Category: Ahmed FR]]
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1RRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRO OCA].
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[[Category: Evans SV]]
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[[Category: Pippy ME]]
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==Reference==
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[[Category: Rose DR]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8487302 8487302]
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[[Category: To R]]
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[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Ahmed, F R.]]
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[[Category: Evans, S V.]]
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[[Category: Pippy, M E.]]
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[[Category: Rose, D R.]]
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[[Category: To, R.]]
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[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:50:01 2008''
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Current revision

REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION

PDB ID 1rro

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