1sch: Difference between revisions

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-[[Image:1sch.gif|left|200px]]
- {{Structure
+==PEANUT PEROXIDASE==
-|PDB= 1sch |SIZE=350|CAPTION= <scene name='initialview01'>1sch</scene>, resolution 2.56&Aring;
+<StructureSection load='1sch' size='340' side='right'caption='[[1sch]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
-|SITE= <scene name='pdbsite=ADC:Distal+Cation+Site+Through+Solvent'>ADC</scene>, <scene name='pdbsite=ADH:Distal+Heme+Pocket'>ADH</scene>, <scene name='pdbsite=APC:Proximal+Cation+Site'>APC</scene>, <scene name='pdbsite=APH:Proximal+Heme+Pocket'>APH</scene>, <scene name='pdbsite=BDC:Distal+Cation+Site+Through+Solvent'>BDC</scene>, <scene name='pdbsite=BDH:Distal+Heme+Pocket'>BDH</scene>, <scene name='pdbsite=BPC:Proximal+Cation+Site'>BPC</scene> and <scene name='pdbsite=BPH:Proximal+Heme+Pocket'>BPH</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
+<table><tr><td colspan='2'>[[1sch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCH FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1sch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sch OCA], [https://pdbe.org/1sch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sch RCSB], [https://www.ebi.ac.uk/pdbsum/1sch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sch ProSAT]</span></td></tr>
+</table>
-'''PEANUT PEROXIDASE'''
+== Function ==
+[https://www.uniprot.org/uniprot/PER1_ARAHY PER1_ARAHY] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent oxidations. Based on sequence alignments, heme peroxidases have been divided into three classes. Crystal structures are available for peroxidases of classes I and II, but until now no structure has been determined for class III, the classical extracellular plant peroxidases. RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7 A resolution. The helical fold is similar to that of known peroxidase structures. The 294-residue polypeptide chain is accompanied by a heme and two calcium ions, and there is some evidence of glycosylation. CONCLUSIONS. This is the first complete structure of a class III peroxidase and as such should serve as a model for other class III enzymes including the much-studied horseradish peroxidase. It may also aid in the interpretation of functional differences between the peroxidase classes. Ten helices conserved in class I and II peroxidases are also found in peanut peroxidase. Key residues of the heme environment and the location of two calcium ions are shared with class II peroxidases. Peanut peroxidase contains three unique helices, two of which contribute to the substrate access channel leading to the heme edge.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1sch_consurf.spt"</scriptWhenChecked>
-SCH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCH OCA].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-The crystal structure of peanut peroxidase., Schuller DJ, Ban N, Huystee RB, McPherson A, Poulos TL, Structure. 1996 Mar 15;4(3):311-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805539 8805539]
+</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=1sch ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Arachis hypogaea]]
-[[Category: Peroxidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Poulos TL]]
-[[Category: Poulos, T L.]]
+[[Category: Schuller DJ]]
-[[Category: Schuller, D J.]]
-[[Category: CA]]
-[[Category: HEM]]
-[[Category: NAG]]
-[[Category: calcium binding]]
-[[Category: glycosylation]]
-[[Category: oxidoreductase]]
-[[Category: peroxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:03:08 2008''