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1rro

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(New page: 200px<br /><applet load="1rro" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rro, resolution 1.3&Aring;" /> '''REFINEMENT OF RECOMBI...)
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[[Image:1rro.jpg|left|200px]]<br /><applet load="1rro" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rro, resolution 1.3&Aring;" />
 
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'''REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION==
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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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<StructureSection load='1rro' size='340' side='right'caption='[[1rro]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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==About this Structure==
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==See Also==
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1RRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1RRO OCA].
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*[[Parvalbumin|Parvalbumin]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8487302 8487302]
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Rattus rattus]]
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[[Category: Single protein]]
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[[Category: Ahmed FR]]
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[[Category: Ahmed, F.R.]]
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[[Category: Evans SV]]
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[[Category: Evans, S.V.]]
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[[Category: Pippy ME]]
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[[Category: Pippy, M.E.]]
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[[Category: Rose DR]]
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[[Category: Rose, D.R.]]
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[[Category: To R]]
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[[Category: To, R.]]
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[[Category: CA]]
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[[Category: calcium-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:49:35 2007''
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Current revision

REFINEMENT OF RECOMBINANT ONCOMODULIN AT 1.30 ANGSTROMS RESOLUTION

PDB ID 1rro

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