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1ycf

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(New page: 200px<br /><applet load="1ycf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ycf, resolution 3.00&Aring;" /> '''Oxidized (di-ferric)...)
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[[Image:1ycf.gif|left|200px]]<br /><applet load="1ycf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ycf, resolution 3.00&Aring;" />
 
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'''Oxidized (di-ferric) FprA from Moorella thermoacetica'''<br />
 
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==Overview==
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==Oxidized (di-ferric) FprA from Moorella thermoacetica==
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Several members of a widespread class of bacterial and archaeal, metalloflavoproteins, called FprA, likely function as scavenging nitric, oxide reductases (S-NORs). However, the only published X-ray crystal, structure of an FprA is for a protein characterized as a, rubredoxin:dioxygen oxidoreductase (ROO) from Desulfovibrio gigas., Therefore, the crystal structure of Moorella thermoacetica FprA, which has, been established to function as an S-NOR, was solved in three different, states: as isolated, reduced, and reduced, NO-reacted. As is the case for, D. gigas ROO, the M. thermoacetica FprA contains a solvent-bridged, non-heme, non-sulfur diiron site with five-coordinate iron centers bridged, by an aspartate, and terminal glutamate, aspartate, and histidine ligands., However, the M. thermoacetica FprA diiron site showed four His ligands, two to each iron, in all three states, whereas the D. gigas ROO diiron, site was reported to contain only three His ligands, even though the, fourth His residue is conserved. The Fe1-Fe2 distance within the diiron, site of M. thermoacetica FprA remained at 3.2-3.4 A with little or no, movement of the protein ligands in the three different states and with, conservation of the two proximal open coordination sites. Molecular, modeling indicated that each open coordination site can accommodate an, end-on NO. This relatively rigid and symmetrical diiron site structure is, consistent with formation of a diferrous dinitrosyl as the committed, catalytic intermediate leading to formation of N(2)O. These results, provide new insight into the structural features that fine-tune biological, non-heme diiron sites for dioxygen activation vs nitric oxide reduction.
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<StructureSection load='1ycf' size='340' side='right'caption='[[1ycf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ycf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YCF FirstGlance]. <br>
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1YCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with ZN, FEO, OXY and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YCF OCA].
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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]] 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=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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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=1ycf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ycf OCA], [https://pdbe.org/1ycf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ycf RCSB], [https://www.ebi.ac.uk/pdbsum/1ycf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ycf ProSAT]</span></td></tr>
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X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase., Silaghi-Dumitrescu R, Kurtz DM Jr, Ljungdahl LG, Lanzilotta WN, Biochemistry. 2005 May 3;44(17):6492-501. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15850383 15850383]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FPRA_MOOTA FPRA_MOOTA] Has nitric oxide reductase activity in combination with Hrb; probably involved in nitrosative stress protection.
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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/yc/1ycf_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=1ycf ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Moorella thermoacetica]]
[[Category: Moorella thermoacetica]]
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[[Category: Single protein]]
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[[Category: Kurtz DM]]
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[[Category: Kurtz, D.M.]]
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[[Category: Lanzilotta WN]]
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[[Category: Lanzilotta, W.N.]]
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[[Category: Silaghi-Dumitrescu R]]
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[[Category: Silaghi-Dumitrescu, R.]]
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[[Category: FEO]]
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[[Category: FMN]]
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[[Category: OXY]]
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[[Category: ZN]]
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[[Category: diferrous-dinitrosyl]]
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[[Category: diron site structure]]
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[[Category: scavenging nitric oxide reductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:40:51 2007''
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Current revision

Oxidized (di-ferric) FprA from Moorella thermoacetica

PDB ID 1ycf

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