2civ

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[[Image:2civ.gif|left|200px]]
 
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==Chloroperoxidase bromide complex==
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The line below this paragraph, containing "STRUCTURE_2civ", creates the "Structure Box" on the page.
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<StructureSection load='2civ' size='340' side='right'caption='[[2civ]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2civ]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CIV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</scene></td></tr>
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{{STRUCTURE_2civ| PDB=2civ | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2civ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2civ OCA], [https://pdbe.org/2civ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2civ RCSB], [https://www.ebi.ac.uk/pdbsum/2civ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2civ ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRXC_LEPFU PRXC_LEPFU] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/2civ_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2civ ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Chloroperoxidase (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.
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'''CHLOROPEROXIDASE BROMIDE COMPLEX'''
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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<ref>PMID:16790441</ref>
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==Overview==
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Chloroperoxidase (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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2CIV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIV OCA].
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</div>
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<div class="pdbe-citations 2civ" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16790441 16790441]
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*[[Haloperoxidase|Haloperoxidase]]
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[[Category: Chloride peroxidase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Leptoxyphium fumago]]
[[Category: Leptoxyphium fumago]]
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[[Category: Single protein]]
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[[Category: Blankenfeldt W]]
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[[Category: Blankenfeldt, W.]]
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[[Category: Kuhnel K]]
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[[Category: Kuhnel, K.]]
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[[Category: Schlichting I]]
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[[Category: Schlichting, I.]]
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[[Category: Terner J]]
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[[Category: Terner, J.]]
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[[Category: Chloride]]
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[[Category: Glycoprotein]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxidase]]
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[[Category: Pyrrolidone carboxylic acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:15:04 2008''
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Current revision

Chloroperoxidase bromide complex

PDB ID 2civ

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