2ohh
From Proteopedia
(New page: 200px<br /><applet load="2ohh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ohh, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:2ohh.jpg|left|200px]]<br /><applet load="2ohh" size=" | + | [[Image:2ohh.jpg|left|200px]]<br /><applet load="2ohh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ohh, resolution 1.70Å" /> | caption="2ohh, resolution 1.70Å" /> | ||
'''Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state'''<br /> | '''Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 FE, SO4 and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: flavodoxine like domain]] | [[Category: flavodoxine like domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:12:20 2008'' |
Revision as of 13:12, 23 January 2008
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Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized state
Overview
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.
About this Structure
2OHH is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with , and as ligands. Full crystallographic information is available from OCA.
Reference
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:17480207
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