1oqu

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(New page: 200px<br /><applet load="1oqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqu, resolution 2.0&Aring;" /> '''A protein coordinated...)
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[[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oqu, resolution 2.0&Aring;" />
 
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'''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes'''<br />
 
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==Overview==
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==A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes==
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The crystal structure of an oxo-centered tri-nuclear iron complex formed, on a protein surface is presented. The cluster forms when crystals of the, class Ib ribonucleotide reductase R2 protein from Corynebacterium, ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is, coordinated by protein-derived carboxylate ligands arranged in a motif, similar to the one found on the inner surface of ferritins and may mimic, an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.
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<StructureSection load='1oqu' size='340' side='right'caption='[[1oqu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oqu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQU 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]] 2&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=1oqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqu OCA], [https://pdbe.org/1oqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqu RCSB], [https://www.ebi.ac.uk/pdbsum/1oqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O69274_CORAM O69274_CORAM] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).[PIRNR:PIRNR000355]
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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/oq/1oqu_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=1oqu 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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1OQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes] with FE, ACT and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA].
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*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization., Hogbom M, Nordlund P, FEBS Lett. 2004 Jun 4;567(2-3):179-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15178319 15178319]
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[[Category: Corynebacterium ammoniagenes]]
[[Category: Corynebacterium ammoniagenes]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hogbom, M.]]
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[[Category: Hogbom M]]
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[[Category: Nordlund, P.]]
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[[Category: Nordlund P]]
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[[Category: ACT]]
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[[Category: FE]]
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[[Category: OXY]]
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[[Category: ferritin]]
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[[Category: glutamate]]
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[[Category: mineralization]]
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[[Category: tri-iron]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:17:28 2007''
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Current revision

A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes

PDB ID 1oqu

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