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[[Image:2ohh.jpg|left|200px]]<br /><applet load="2ohh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ohh, resolution 1.70&Aring;" />
'''Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state'''<br />


==Overview==
==Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state==
The di-iron flavoprotein F(420)H(2) oxidase found in methanogenic Archaea, catalyzes the four-electron reduction of O(2) to 2H(2)O with 2 mol of, reduced coenzyme F(420)(7,8-dimethyl-8-hydroxy-5-deazariboflavin). We, report here on crystal structures of the homotetrameric F(420)H(2) oxidase, from Methanothermobacter marburgensis at resolutions of 2.25 A, 2.25 A and, 1.7 A, respectively, from which an active reduced state, an inactive, oxidized state and an active oxidized state could be extracted. As found, in structurally related A-type flavoproteins, the active site is formed at, the dimer interface, where the di-iron center of one monomer is juxtaposed, to FMN of the other. In the active reduced state [Fe(II)Fe(II)FMNH(2)], the two irons are surrounded by four histidines, one aspartate, one, glutamate and one bridging aspartate. The so-called switch loop is in a, closed conformation, thus preventing F(420) binding. In the inactive, oxidized state [Fe(III)FMN], the iron nearest to FMN has moved to two, remote binding sites, and the switch loop is changed to an open, conformation. In the active oxidized state [Fe(III)Fe(III)FMN], both irons, are positioned as in the reduced state but the switch loop is found in the, open conformation as in the inactive oxidized state. It is proposed that, the redox-dependent conformational change of the switch loop ensures, alternate complete four-electron O(2) reduction and redox center, re-reduction. On the basis of the known Si-Si stereospecific hydride, transfer, F(420)H(2) was modeled into the solvent-accessible pocket in, front of FMN. The inactive oxidized state might provide the molecular, basis for enzyme inactivation by long-term O(2) exposure observed in some, members of the FprA family.
<StructureSection load='2ohh' size='340' side='right'caption='[[2ohh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2ohh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OHH FirstGlance]. <br>
2OHH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHH OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ohh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ohh OCA], [https://pdbe.org/2ohh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ohh RCSB], [https://www.ebi.ac.uk/pdbsum/2ohh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ohh ProSAT]</span></td></tr>
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O., Seedorf H, Hagemeier CH, Shima S, Thauer RK, Warkentin E, Ermler U, FEBS J. 2007 Mar;274(6):1588-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17480207 17480207]
</table>
== Function ==
[https://www.uniprot.org/uniprot/FPRA_METTM FPRA_METTM] Probably functions as an electron acceptor for a hydrogenase; however there is an uncharacterized intermediate between the hydrogenase and flavoprotein A.<ref>PMID:9660187</ref>
== 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/oh/2ohh_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=2ohh ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Single protein]]
[[Category: Ermler U]]
[[Category: Ermler, U.]]
[[Category: Seedorf H]]
[[Category: Seedorf, H.]]
[[Category: Warkentin E]]
[[Category: Warkentin, E.]]
[[Category: FE]]
[[Category: FMN]]
[[Category: SO4]]
[[Category: beta-lactamase like domain]]
[[Category: flavodoxine like domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:12:20 2008''

Latest revision as of 06:29, 3 April 2024

Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state

2ohh, resolution 1.70Å

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