1vm9
From Proteopedia
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| - | [[Image:1vm9.png|left|200px]] | ||
| - | + | ==The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1== | |
| + | <StructureSection load='1vm9' size='340' side='right'caption='[[1vm9]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1vm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VM9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1vm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vm9 OCA], [https://pdbe.org/1vm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vm9 RCSB], [https://www.ebi.ac.uk/pdbsum/1vm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vm9 ProSAT], [https://www.topsan.org/Proteins/CESG/1vm9 TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TMOC_PSEME TMOC_PSEME] Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/1vm9_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1vm9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The structure of the Rieske-type ferredoxin (T4moC) from toluene 4-monooxygenase was determined by X-ray crystallography in the [2Fe-2S](2+) state at a resolution of 1.48 A using single-wavelength anomalous dispersion phasing with the [2Fe-2S] center. The structure consists of ten beta-strands arranged into the three antiparallel beta-sheet topology observed in all Rieske proteins. Trp69 of T4moC is adjacent to the [2Fe-2S] centre, which displaces a loop containing the conserved Pro81 by approximately 8 A away from the [2Fe-2S] cluster compared with the Pro loop in the closest structural and functional homolog, the Rieske-type ferredoxin BphF from biphenyl dioxygenase. In addition, T4moC contains five hydrogen bonds to the [2Fe-2S] cluster compared with three hydrogen bonds in BphF. Moreover, the electrostatic surface of T4moC is distinct from that of BphF. These structural differences are identified as possible contributors to the evolutionary specialization of soluble Rieske-type ferredoxins between the diiron monooxygenases and cis-dihydrodiol-forming dioxygenases. | ||
| - | + | Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-monooxygenase.,Moe LA, Bingman CA, Wesenberg GE, Phillips GN Jr, Fox BG Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):476-82. Epub 2006, Apr 19. PMID:16627939<ref>PMID:16627939</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1vm9" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Ferredoxin|Ferredoxin]] | + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| - | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pseudomonas mendocina]] | [[Category: Pseudomonas mendocina]] | ||
| - | [[Category: Allard | + | [[Category: Allard STM]] |
| - | [[Category: Bingman | + | [[Category: Bingman CA]] |
| - | + | [[Category: Fox BG]] | |
| - | [[Category: Fox | + | [[Category: Moe LA]] |
| - | [[Category: Moe | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Phillips | + | [[Category: Smith DW]] |
| - | [[Category: Smith | + | [[Category: Wesenberg GE]] |
| - | [[Category: Wesenberg | + | |
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Current revision
The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1
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