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[[Image:1brt.jpg|left|200px]]
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{{STRUCTURE_1brt|  PDB=1brt  |  SCENE=  }}
'''BROMOPEROXIDASE A2 MUTANT M99T'''


==BROMOPEROXIDASE A2 MUTANT M99T==
<StructureSection load='1brt' size='340' side='right'caption='[[1brt]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1brt]] 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=1BRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1brt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brt OCA], [https://pdbe.org/1brt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brt RCSB], [https://www.ebi.ac.uk/pdbsum/1brt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BPOA2_KITAU BPOA2_KITAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brt_consurf.spt"</scriptWhenChecked>
    <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=1brt 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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BRT 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=1BRT OCA].
</div>
<div class="pdbe-citations 1brt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Haloperoxidase|Haloperoxidase]]
[[Category: Chloride peroxidase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Streptomyces aureofaciens]]
__TOC__
[[Category: Altenbuchner, J.]]
</StructureSection>
[[Category: Hecht, H J.]]
[[Category: Kitasatospora aureofaciens]]
[[Category: Hofmann, B.]]
[[Category: Large Structures]]
[[Category: Pee, K H.Van.]]
[[Category: Altenbuchner J]]
[[Category: Pelletier, I.]]
[[Category: Hecht HJ]]
[[Category: Toelzer, S.]]
[[Category: Hofmann B]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Pelletier I]]
[[Category: Haloperoxidase]]
[[Category: Toelzer S]]
[[Category: Mutant m99t]]
[[Category: Van Pee KH]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:52:45 2008''
Retrieved from "https://proteopedia.org/1brt"