2j19

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[[Image:2j19.jpg|left|200px]]<br /><applet load="2j19" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j19, resolution 1.750&Aring;" />
 
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'''FERROUS CHLOROPEROXIDASE (HIGH DOSE DATA SET)'''<br />
 
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==Overview==
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==Ferrous Chloroperoxidase (high dose data set)==
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<StructureSection load='2j19' size='340' side='right'caption='[[2j19]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j19]] 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=2J19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J19 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]] 1.75&#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=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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j19 OCA], [https://pdbe.org/2j19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j19 RCSB], [https://www.ebi.ac.uk/pdbsum/2j19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j19 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/j1/2j19_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=2j19 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 ==
The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed.
The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed.
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==About this Structure==
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Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography.,Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:17211068<ref>PMID:17211068</ref>
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2J19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Br+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J19 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography., Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I, J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17211068 17211068]
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</div>
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[[Category: Chloride peroxidase]]
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<div class="pdbe-citations 2j19" style="background-color:#fffaf0;"></div>
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[[Category: Leptoxyphium fumago]]
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[[Category: Single protein]]
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[[Category: Beitlich, T.]]
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[[Category: Kuhnel, K.]]
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[[Category: Schlichting, I.]]
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[[Category: Schulze-Briese, C.]]
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[[Category: Shoeman, R L.]]
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[[Category: BR]]
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[[Category: HEM]]
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[[Category: MAN]]
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[[Category: MN]]
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[[Category: NAG]]
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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 Thu Feb 21 17:58:15 2008''
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==See Also==
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*[[Haloperoxidase|Haloperoxidase]]
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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]]
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[[Category: Leptoxyphium fumago]]
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[[Category: Beitlich T]]
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[[Category: Kuhnel K]]
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[[Category: Schlichting I]]
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[[Category: Schulze-Briese C]]
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[[Category: Shoeman RL]]

Current revision

Ferrous Chloroperoxidase (high dose data set)

PDB ID 2j19

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