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PDBsum entry 1sb3

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1sb3
Jmol
Contents
Protein chains
761 a.a. *
323 a.a. *
161 a.a. *
Ligands
PCD ×2
EPE
FAD ×2
SF4 ×2
FES ×4
SO4 ×2
Waters ×1042
* Residue conservation analysis
PDB id:
1sb3
Name: Oxidoreductase
Title: Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica
Structure: 4-hydroxybenzoyl-coa reductase alpha subunit. Chain: a, d. 4-hydroxybenzoyl-coa reductase beta subunit. Chain: b, e. 4-hydroxybenzoyl-coa reductase gamma subunit. Chain: c, f. Ec: 1.3.99.20
Source: Thauera aromatica. Organism_taxid: 59405. Strain: strain k, dsmz 6984. Strain: strain k, dsmz 6984
Biol. unit: Hexamer (from PQS)
Resolution:
2.20Å     R-factor:   0.171     R-free:   0.205
Authors: M.Unciuleac,E.Warkentin,C.C.Page,M.Boll,U.Ermler
Key ref:
M.Unciuleac et al. (2004). Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow. Structure, 12, 2249-2256. PubMed id: 15576037 DOI: 10.1016/j.str.2004.10.008
Date:
10-Feb-04     Release date:   21-Dec-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O33819  (HCRA_THAAR) -  4-hydroxybenzoyl-CoA reductase subunit alpha
Seq:
Struc:
 
Seq:
Struc:
769 a.a.
761 a.a.*
Protein chains
Pfam   ArchSchema ?
O33820  (HCRB_THAAR) -  4-hydroxybenzoyl-CoA reductase subunit beta
Seq:
Struc:
324 a.a.
323 a.a.
Protein chains
Pfam   ArchSchema ?
O33818  (HCRC_THAAR) -  4-hydroxybenzoyl-CoA reductase subunit gamma
Seq:
Struc:
161 a.a.
161 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F: E.C.1.3.7.9  - 4-hydroxybenzoyl-CoA reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Benzoyl-CoA + oxidized ferredoxin = 4-hydroxybenzoyl-CoA + reduced ferredoxin
Benzoyl-CoA
Bound ligand (Het Group name = FAD)
matches with 43.00% similarity
+ oxidized ferredoxin
= 4-hydroxybenzoyl-CoA
+ reduced ferredoxin
      Cofactor: Flavin; Iron-sulfur; Mo cation
Flavin
Iron-sulfur
Mo cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     catalytic activity     11 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.str.2004.10.008 Structure 12:2249-2256 (2004)
PubMed id: 15576037  
 
 
Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow.
M.Unciuleac, E.Warkentin, C.C.Page, M.Boll, U.Ermler.
 
  ABSTRACT  
 
The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic degradation of phenolic compounds and belongs to the xanthine oxidase (XO) family of molybdenum enzymes. Its X-ray structure was established at 1.6 A resolution. The most pronounced difference between 4-HBCR and other structurally characterized members of the XO family is the insertion of 40 amino acids within cluster at a distance of 16.5 A to the isoalloxazine ring of FAD. The architecture of 4-HBCR and concomitantly performed electron transfer rate calculations suggest an inverted cluster to the Mo over a distance of 55 A. The binding site of 4-hydroxybenzoyl-CoA is located in an 18 A long channel lined up by several aromatic side chains around the aromatic moiety, which are proposed to shield and stabilize the postulated radical intermediates during catalysis.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Reaction Catalyzed by 4-Hydroxybenzoyl-CoA Reductase

 
  The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 2249-2256) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21151514 M.Neumann, and S.Leimkühler (2011).
The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria.
  Biochem Res Int, 2011, 850924.  
19258534 M.Carmona, M.T.Zamarro, B.Blázquez, G.Durante-Rodríguez, J.F.Juárez, J.A.Valderrama, M.J.Barragán, J.L.García, and E.Díaz (2009).
Anaerobic catabolism of aromatic compounds: a genetic and genomic view.
  Microbiol Mol Biol Rev, 73, 71.  
19452052 M.J.Romão (2009).
Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview.
  Dalton Trans, (), 4053-4068.  
18378589 G.Fuchs (2008).
Anaerobic metabolism of aromatic compounds.
  Ann N Y Acad Sci, 1125, 82-99.  
18658262 J.Johannes, A.Bluschke, N.Jehmlich, M.von Bergen, and M.Boll (2008).
Purification and characterization of active-site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens.
  J Bacteriol, 190, 6493-6500.  
17449613 F.Peters, D.Heintz, J.Johannes, A.van Dorsselaer, and M.Boll (2007).
Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens.
  J Bacteriol, 189, 4729-4738.  
16480912 C.D.Brondino, M.J.Romão, I.Moura, and J.J.Moura (2006).
Molybdenum and tungsten enzymes: the xanthine oxidase family.
  Curr Opin Chem Biol, 10, 109-114.  
16704345 W.Buckel, and B.T.Golding (2006).
Radical enzymes in anaerobes.
  Annu Rev Microbiol, 60, 27-49.  
16218872 M.Boll, B.Schink, A.Messerschmidt, and P.M.Kroneck (2005).
Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism.
  Biol Chem, 386, 999.  
16218871 M.Boll, and G.Fuchs (2005).
Unusual reactions involved in anaerobic metabolism of phenolic compounds.
  Biol Chem, 386, 989-997.  
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.