2j18: Difference between revisions

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-[[Image:2j18.jpg|left|200px]]
- {{Structure
+==Chloroperoxidase mixture of ferric and ferrous states (low dose data set)==
-|PDB= 2j18 |SIZE=350|CAPTION= <scene name='initialview01'>2j18</scene>, resolution 1.75&Aring;
+<StructureSection load='2j18' size='340' side='right'caption='[[2j18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Br+Binding+Site+For+Chain+A'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <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>
+<table><tr><td colspan='2'>[[2j18]] 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=2J18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J18 FirstGlance]. <br>
-|ACTIVITY= <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='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>
-|GENE=
+<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></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [https://pdbe.org/2j18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB], [https://www.ebi.ac.uk/pdbsum/2j18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j18 ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j18 OCA], [http://www.ebi.ac.uk/pdbsum/2j18 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j18 RCSB]</span>
+== Function ==
-}}
+[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.
+== 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/j1/2j18_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2j18 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-'''CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW DOSE DATA SET)'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2j18" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Haloperoxidase|Haloperoxidase]]
+== References ==
-==About this Structure==
+<references/>
-J18 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=2J18 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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://www.ncbi.nlm.nih.gov/pubmed/17211068 17211068]
-[[Category: Chloride peroxidase]]
 [[Category: Leptoxyphium fumago]]
-[[Category: Single protein]]
+[[Category: Beitlich T]]
-[[Category: Beitlich, T.]]
+[[Category: Kuhnel K]]
-[[Category: Kuhnel, K.]]
+[[Category: Schlichting I]]
-[[Category: Schlichting, I.]]
+[[Category: Schulze-Briese C]]
-[[Category: Schulze-Briese, C.]]
+[[Category: Shoeman RL]]
-[[Category: Shoeman, R L.]]
-[[Category: chloride]]
-[[Category: glycoprotein]]
-[[Category: heme]]
-[[Category: iron]]
-[[Category: manganese]]
-[[Category: metal-binding]]
-[[Category: oxidoreductase]]
-[[Category: peroxidase]]
-[[Category: pyrrolidone carboxylic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:42 2008''