2cj2: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cpo|1cpo]], [[2civ|2civ]], [[2ciw|2ciw]], [[2cix|2cix]], [[2ciy|2ciy]], [[2ciz|2ciz]], [[2cj0|2cj0]], [[2cj1|2cj1]], [[2cpo|2cpo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cpo|1cpo]], [[2civ|2civ]], [[2ciw|2ciw]], [[2cix|2cix]], [[2ciy|2ciy]], [[2ciz|2ciz]], [[2cj0|2cj0]], [[2cj1|2cj1]], [[2cpo|2cpo]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cj2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2cj2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cj2 OCA], [http://pdbe.org/2cj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cj2 RCSB], [http://www.ebi.ac.uk/pdbsum/2cj2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2cj2" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 03:17, 10 September 2015
CHLOROPEROXIDASE COMPLEXED WITH FORMATE (SUGAR CRYOPROTECTANT)CHLOROPEROXIDASE COMPLEXED WITH FORMATE (SUGAR CRYOPROTECTANT)
Structural highlights
Function[PRXC_CALFU] Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases. 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 PubMedChloroperoxidase (CPO) is a heme-thiolate enzyme that catalyzes hydrogen peroxide-dependent halogenation reactions. Structural data on substrate binding have not been available so far. CPO was therefore crystallized in the presence of iodide or bromide. One halide binding site was identified at the surface near a narrow channel that connects the surface with the heme. Two other halide binding sites were identified within and at the other end of this channel. Together, these sites suggest a pathway for access of halide anions to the active site. The structure of CPO complexed with its natural substrate cyclopentanedione was determined at a resolution of 1.8 A. This is the first example of a CPO structure with a bound organic substrate. In addition, structures of CPO bound with nitrate, acetate, and formate and of a ternary complex with dimethylsulfoxide (Me2SO) and cyanide were determined. These structures have implications for the mechanism of compound I formation. Before binding to the heme, the incoming hydrogen peroxide first interacts with Glu-183. The deprotonated Glu-183 abstracts a proton from hydrogen peroxide. The hydroperoxo-anion then binds at the heme, yielding compound 0. Glu-183 protonates the distal oxygen of compound 0, water is released, and compound I is formed. Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.,Kuhnel K, Blankenfeldt W, Terner J, Schlichting I J Biol Chem. 2006 Aug 18;281(33):23990-8. Epub 2006 Jun 20. PMID:16790441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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