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PDBsum entry 2ohi

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2ohi
Jmol
Contents
Protein chains
(+ 2 more) 403 a.a. *
Ligands
FMN ×8
Metals
_FE ×16
_CL ×4
Waters ×365
* Residue conservation analysis
PDB id:
2ohi
Name: Oxidoreductase
Title: Crystal structure of coenzyme f420h2 oxidase (fpra), a diiro flavoprotein, reduced state
Structure: Type a flavoprotein fpra. Chain: a, b, d, e, g, h, i, j. Synonym: fmn-protein fpra, flavoprotein a. Engineered: yes
Source: Methanothermobacter thermautotrophicus organism_taxid: 145262. Strain: dszm2133. Gene: fpra, fpaa. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.30Å     R-factor:   0.206     R-free:   0.269
Authors: H.Seedorf,E.Warkentin,U.Ermler
Key ref: H.Seedorf et al. (2007). Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O. FEBS J, 274, 1588-1599. PubMed id: 17480207
Date:
10-Jan-07     Release date:   22-May-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q50497  (FPRA_METTM) -  Type A flavoprotein FprA
Seq:
Struc:
404 a.a.
403 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     electron carrier activity     6 terms  

 

 
FEBS J 274:1588-1599 (2007)
PubMed id: 17480207  
 
 
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O.
H.Seedorf, C.H.Hagemeier, S.Shima, R.K.Thauer, E.Warkentin, U.Ermler.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19337761 B.L.Victor, A.M.Baptista, and C.M.Soares (2009).
Dioxygen and nitric oxide pathways and affinity to the catalytic site of rubredoxin:oxygen oxidoreductase from Desulfovibrio gigas.
  J Biol Inorg Chem, 14, 853-862.  
19011120 T.Smutná, V.L.Gonçalves, L.M.Saraiva, J.Tachezy, M.Teixeira, and I.Hrdy (2009).
Flavodiiron protein from Trichomonas vaginalis hydrogenosomes: the terminal oxygen reductase.
  Eukaryot Cell, 8, 47-55.  
18077462 A.Di Matteo, F.M.Scandurra, F.Testa, E.Forte, P.Sarti, M.Brunori, and A.Giuffrè (2008).
The O2-scavenging flavodiiron protein in the human parasite Giardia intestinalis.
  J Biol Chem, 283, 4061-4068.
PDB code: 2q9u
18786405 M.V.Petoukhov, J.B.Vicente, P.B.Crowley, M.A.Carrondo, M.Teixeira, and D.I.Svergun (2008).
Quaternary structure of flavorubredoxin as revealed by synchrotron radiation small-angle X-ray scattering.
  Structure, 16, 1428-1436.  
17961173 A.Tholen, M.Pester, and A.Brune (2007).
Simultaneous methanogenesis and oxygen reduction by Methanobrevibacter cuticularis at low oxygen fluxes.
  FEMS Microbiol Ecol, 62, 303-312.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.