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[[Image:1a8q.gif|left|200px]]


{{Structure
==BROMOPEROXIDASE A1==
|PDB= 1a8q |SIZE=350|CAPTION= <scene name='initialview01'>1a8q</scene>, resolution 1.75&Aring;
<StructureSection load='1a8q' size='340' side='right'caption='[[1a8q]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
|SITE= <scene name='pdbsite=NUL:Catalytic+Triad'>NUL</scene>
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1a8q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8Q FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
|GENE= BPOA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1894 Streptomyces aureofaciens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8q OCA], [https://pdbe.org/1a8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8q RCSB], [https://www.ebi.ac.uk/pdbsum/1a8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8q ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8q OCA], [http://www.ebi.ac.uk/pdbsum/1a8q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a8q RCSB]</span>
[https://www.uniprot.org/uniprot/CPOA1_KITAU CPOA1_KITAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Able to brominate as well.<ref>PMID:1783900</ref>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''BROMOPEROXIDASE A1'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8q_consurf.spt"</scriptWhenChecked>
==Overview==
    <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=1a8q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.
The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.


==About this Structure==
Structural investigation of the cofactor-free chloroperoxidases.,Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069<ref>PMID:9642069</ref>
1A8Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_aureofaciens Streptomyces aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Q OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural investigation of the cofactor-free chloroperoxidases., Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ, J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9642069 9642069]
</div>
[[Category: Chloride peroxidase]]
<div class="pdbe-citations 1a8q" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Streptomyces aureofaciens]]
[[Category: Altenbuchner, J.]]
[[Category: Hecht, H J.]]
[[Category: Hofmann, B.]]
[[Category: Pee, K H.Van.]]
[[Category: Pelletier, I.]]
[[Category: Toelzer, S.]]
[[Category: haloperoxidase]]
[[Category: oxidoreductase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:35:38 2008''
==See Also==
*[[Haloperoxidase|Haloperoxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kitasatospora aureofaciens]]
[[Category: Large Structures]]
[[Category: Altenbuchner J]]
[[Category: Hecht H-J]]
[[Category: Hofmann B]]
[[Category: Pelletier I]]
[[Category: Toelzer S]]
[[Category: Van Pee K-H]]

Latest revision as of 13:49, 2 August 2023

BROMOPEROXIDASE A1BROMOPEROXIDASE A1

Structural highlights

1a8q is a 1 chain structure with sequence from Kitasatospora aureofaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CPOA1_KITAU May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Able to brominate as well.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.

Structural investigation of the cofactor-free chloroperoxidases.,Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Weng M, Pfeifer O, Krauss S, Lingens F, van Pée KH. Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762. J Gen Microbiol. 1991 Nov;137(11):2539-46. PMID:1783900 doi:10.1099/00221287-137-11-2539
  2. ↑ Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ. Structural investigation of the cofactor-free chloroperoxidases. J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069 doi:http://dx.doi.org/10.1006/jmbi.1998.1802

1a8q, resolution 1.75Å

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