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Haloperoxidase PDB id
1bro
Jmol
Contents
Protein chains
277 a.a. *
Waters ×235
* Residue conservation analysis
PDB id:
1bro
Name: Haloperoxidase
Title: Bromoperoxidase a2
Structure: Bromoperoxidase a2. Chain: a, b. Synonym: haloperoxidase a2, chloroperoxidase a2. Engineered: yes
Source: Streptomyces aureofaciens. Organism_taxid: 1894. Atcc: 10762. Gene: bpoa2. Expressed in: streptomyces lividans. Expression_system_taxid: 1916.
Biol. unit: Trimer (from PDB file)
Resolution:
2.05Å     R-factor:   0.184    
Authors: H.J.Hecht,H.Sobek,T.Haag,O.Pfeifer,K.H.Van Pee
Key ref: H.J.Hecht et al. (1994). The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold. Nat Struct Biol, 1, 532-537. PubMed id: 7664081 DOI: 10.1038/nsb0894-532
Date:
01-Jun-96     Release date:   07-Dec-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P29715  (BPOA2_STRAU) -  Non-haem bromoperoxidase BPO-A2
Seq:
Struc: 		278 a.a.
277 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation reduction   2 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
DOI no: 10.1038/nsb0894-532 Nat Struct Biol 1:532-537 (1994)
PubMed id: 7664081  
 
 
The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
H.J.Hecht, H.Sobek, T.Haag, O.Pfeifer, K.H.van Pée.
 
  ABSTRACT  
 
The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20693690 J.M.Johnston, M.Jiang, Z.Guo, and E.N.Baker (2010).
Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis.
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PDB codes: 3e3a 3hss 3hys
20080731 R.A.Steiner, H.J.Janssen, P.Roversi, A.J.Oakley, and S.Fetzner (2010).
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold.
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PDB codes: 2wj3 2wj4 2wj6 2wm2 3ibt
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Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes.
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15632289 T.Kaneko, N.Tanaka, and T.Kumasaka (2005).
Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis.
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PDB codes: 1wom 1wpr
14672934 B.Padmanabhan, T.Kuzuhara, N.Adachi, and M.Horikoshi (2004).
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Crystal structure of aclacinomycin methylesterase with bound product analogues: implications for anthracycline recognition and mechanism.
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PDB codes: 1q0r 1q0z
12892883 R.De Mot, A.De Schrijver, G.Schoofs, and A.H.Parret (2003).
The thiocarbamate-inducible Rhodococcus enzyme ThcF as a member of the family of alpha/beta hydrolases with haloperoxidative side activity.
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  11880037 O.Puk, P.Huber, D.Bischoff, J.Recktenwald, G.Jung, R.D.Süssmuth, K.H.van Pée, W.Wohlleben, and S.Pelzer (2002).
Glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908: function of a halogenase and a haloperoxidase/perhydrolase.
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12007643 U.T.Bornscheuer (2002).
Microbial carboxyl esterases: classification, properties and application in biocatalysis.
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Natural halogenated fatty acids: their analogues and derivatives.
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11238985 K.S.Makarova, L.Aravind, Y.I.Wolf, R.L.Tatusov, K.W.Minton, E.V.Koonin, and M.J.Daly (2001).
Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics.
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11591687 M.S.Brody, K.Vijay, and C.W.Price (2001).
Catalytic function of an alpha/beta hydrolase is required for energy stress activation of the sigma(B) transcription factor in Bacillus subtilis.
  J Bacteriol, 183, 6422-6428.  
19153837 G.W.Gribble (2000).
The natural production of organobromine compounds.
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  10673439 J.Zou, B.M.Hallberg, T.Bergfors, F.Oesch, M.Arand, S.L.Mowbray, and T.A.Jones (2000).
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  Structure, 8, 111-122.
PDB code: 1qo7
10722044 K.H.van Pée, S.Keller, T.Wage, I.Wynands, H.Schnerr, and S.Zehner (2000).
Enzymatic halogenation catalyzed via a catalytic triad and by oxidoreductases.
  Biol Chem, 381, 1-5.  
  10338021 B.Zhang, L.Rychlewski, K.Pawłowski, J.S.Fetrow, J.Skolnick, and A.Godzik (1999).
From fold predictions to function predictions: automation of functional site conservation analysis for functional genome predictions.
  Protein Sci, 8, 1104-1115.  
10494857 E.Henke, and U.T.Bornscheuer (1999).
Directed evolution of an esterase from Pseudomonas fluorescens. Random mutagenesis by error-prone PCR or a mutator strain and identification of mutants showing enhanced enantioselectivity by a resorufin-based fluorescence assay.
  Biol Chem, 380, 1029-1033.  
  10482514 F.Fischer, S.Künne, and S.Fetzner (1999).
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.
  J Bacteriol, 181, 5725-5733.  
9989236 F.Morel, C.Gilbert, C.Geourjon, J.Frot-Coutaz, R.Portalier, and D.Atlan (1999).
The prolyl aminopeptidase from Lactobacillus delbrueckii subsp. bulgaricus belongs to the alpha/beta hydrolase fold family.
  Biochim Biophys Acta, 1429, 501-505.  
  10021409 J.Littlechild (1999).
Haloperoxidases and their role in biotransformation reactions.
  Curr Opin Chem Biol, 3, 28-34.  
10329649 M.Nardini, I.S.Ridder, H.J.Rozeboom, K.H.Kalk, R.Rink, D.B.Janssen, and B.W.Dijkstra (1999).
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides.
  J Biol Chem, 274, 14579-14586.
PDB code: 1ehy
10350631 N.Max, A.Betz, S.Facey, F.Lingens, B.Hauer, and S.Fetzner (1999).
Cloning, sequence analysis, and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase.
  Biochim Biophys Acta, 1431, 547-552.  
  9925571 V.Khalameyzer, I.Fischer, U.T.Bornscheuer, and J.Altenbuchner (1999).
Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones.
  Appl Environ Microbiol, 65, 477-482.  
9720251 J.Pleiss, M.Fischer, and R.D.Schmid (1998).
Anatomy of lipase binding sites: the scissile fatty acid binding site.
  Chem Phys Lipids, 93, 67-80.  
9722515 S.Y.Seah, G.Terracina, J.T.Bolin, P.Riebel, V.Snieckus, and L.D.Eltis (1998).
Purification and preliminary characterization of a serine hydrolase involved in the microbial degradation of polychlorinated biphenyls.
  J Biol Chem, 273, 22943-22949.  
  9562561 Y.Wei, L.Swenson, C.Castro, U.Derewenda, W.Minor, H.Arai, J.Aoki, K.Inoue, L.Servin-Gonzalez, and Z.S.Derewenda (1998).
Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 A resolution.
  Structure, 6, 511-519.
PDB code: 1jfr
  9143122 A.De Schrijver, I.Nagy, G.Schoofs, P.Proost, J.Vanderleyden, K.H.van Pée, and R.De Mot (1997).
Thiocarbamate herbicide-inducible nonheme haloperoxidase of Rhodococcus erythropolis NI86/21.
  Appl Environ Microbiol, 63, 1911-1916.  
9151984 F.Müller, M.Arand, H.Frank, A.Seidel, W.Hinz, L.Winkler, K.Hänel, E.Blée, J.K.Beetham, B.D.Hammock, and F.Oesch (1997).
Visualization of a covalent intermediate between microsomal epoxide hydrolase, but not cholesterol epoxide hydrolase, and their substrates.
  Eur J Biochem, 245, 490-496.  
9341166 M.Karlsson, J.A.Contreras, U.Hellman, H.Tornqvist, and C.Holm (1997).
cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases.
  J Biol Chem, 272, 27218-27223.  
9310385 P.A.Kroon, C.B.Faulds, C.Brézillon, and G.Williamson (1997).
Methyl phenylalkanoates as substrates to probe the active sites of esterases.
  Eur J Biochem, 248, 245-251.  
8552646 A.Messerschmidt, and R.Wever (1996).
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
  Proc Natl Acad Sci U S A, 93, 392-396.
PDB code: 1vnc
8905085 K.H.van Pée (1996).
Biosynthesis of halogenated metabolites by bacteria.
  Annu Rev Microbiol, 50, 375-399.  
8626766 M.Arand, H.Wagner, and F.Oesch (1996).
Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase.
  J Biol Chem, 271, 4223-4229.  
  8805565 U.G.Wagner, M.Hasslacher, H.Griengl, H.Schwab, and C.Kratky (1996).
Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis.
  Structure, 4, 811-822.
PDB code: 1yas
8552644 Y.Chen, J.Inobe, V.K.Kuchroo, J.L.Baron, C.A.Janeway, and H.L.Weiner (1996).
Oral tolerance in myelin basic protein T-cell receptor transgenic mice: suppression of autoimmune encephalomyelitis and dose-dependent induction of regulatory cells.
  Proc Natl Acad Sci U S A, 93, 388-391.  
7744081 B.H.Simons, P.Barnett, E.G.Vollenbroek, H.L.Dekker, A.O.Muijsers, A.Messerschmidt, and R.Wever (1995).
Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis.
  Eur J Biochem, 229, 566-574.  
7607409 W.Burd, O.Yourkevich, A.J.Voskoboev, and K.H.van Pée (1995).
Purification and properties of a non-haem chloroperoxidase from Serratia marcescens.
  FEMS Microbiol Lett, 129, 255-260.  
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 codes are shown on the right.