1a88: Difference between revisions

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[[Image:1a88.jpg|left|200px]]
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{{STRUCTURE_1a88|  PDB=1a88  |  SCENE=  }}
'''CHLOROPEROXIDASE L'''


==CHLOROPEROXIDASE L==
<StructureSection load='1a88' size='340' side='right'caption='[[1a88]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a88]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A88 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]] 1.9&#8491;</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=1a88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a88 OCA], [https://pdbe.org/1a88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a88 RCSB], [https://www.ebi.ac.uk/pdbsum/1a88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a88 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRXC_STRLI PRXC_STRLI]
== 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/a8/1a88_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=1a88 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>
1A88 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A88 OCA].
</div>
<div class="pdbe-citations 1a88" 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/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: Altenbuchner, J.]]
[[Category: Altenbuchner J]]
[[Category: Hecht, H J.]]
[[Category: Hecht H-J]]
[[Category: Hofmann, B.]]
[[Category: Hofmann B]]
[[Category: Pee, K H.Van.]]
[[Category: Pelletier I]]
[[Category: Pelletier, I.]]
[[Category: Toelzer S]]
[[Category: Toelzer, S.]]
[[Category: Van Pee K-H]]
[[Category: Haloperoxidase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:57:37 2008''
Retrieved from "https://proteopedia.org/1a88"