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==BROMOPEROXIDASE A1== | ==BROMOPEROXIDASE A1== | ||
<StructureSection load='1a8q' size='340' side='right' caption='[[1a8q]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1a8q' size='340' side='right'caption='[[1a8q]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a8q]] is a 1 chain structure with sequence from [ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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=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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8q_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8q_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 29: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1a8q" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1a8q" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Haloperoxidase|Haloperoxidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Kitasatospora aureofaciens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Altenbuchner | [[Category: Altenbuchner J]] | ||
[[Category: Hecht | [[Category: Hecht H-J]] | ||
[[Category: Hofmann | [[Category: Hofmann B]] | ||
[[Category: Pelletier I]] | |||
[[Category: Pelletier | [[Category: Toelzer S]] | ||
[[Category: Toelzer | [[Category: Van Pee K-H]] | ||
[[Category: | |||
Latest revision as of 13:49, 2 August 2023
BROMOPEROXIDASE A1BROMOPEROXIDASE A1
Structural highlights
FunctionCPOA1_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 PubMedThe 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 AlsoReferences
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