1jdr: Difference between revisions

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-[[Image:1jdr.jpg|left|200px]]
- {{Structure
+==Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase==
-|PDB= 1jdr |SIZE=350|CAPTION= <scene name='initialview01'>1jdr</scene>, resolution 1.5&Aring;
+<StructureSection load='1jdr' size='340' side='right'caption='[[1jdr]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
+<table><tr><td colspan='2'>[[1jdr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDR FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </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]] 1.5&#8491;</td></tr>
-|GENE= OPBYC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1jdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdr OCA], [https://pdbe.org/1jdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdr RCSB], [https://www.ebi.ac.uk/pdbsum/1jdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdr ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdr OCA], [http://www.ebi.ac.uk/pdbsum/1jdr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdr RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
+== 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/jd/1jdr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1jdr ConSurf].
+<div style="clear:both"></div>
-'''Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase'''
+==See Also==
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Earlier work [Bonagura et al. (1996) Biochemistry 35, 6107] showed that the K+ site found in the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (CCP). Binding of K+ at the engineered site results in a loss in activity and destabilization of the CCP compound I Trp191 cationic radical owing to long-range electrostatic effects. The engineered CCP mutant crystal structure has been refined to 1.5 A using data obtained at cryogenic temperatures which provides a more detailed basis for comparison with the naturally occurring K+ site in APX. The characteristic EPR signal associated with the Trp191 radical becomes progressively weaker as K+ is added, which correlates well with the loss in enzyme activity as [K+] is increased. These results coupled with stopped-flow studies support our earlier conclusions that the loss in activity and EPR signal is due to destabilization of the Trp191 cationic radical.
+[[Category: Large Structures]]
-==About this Structure==
-JDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDR OCA].
-==Reference==
-The effects of an engineered cation site on the structure, activity, and EPR properties of cytochrome c peroxidase., Bonagura CA, Sundaramoorthy M, Bhaskar B, Poulos TL, Biochemistry. 1999 Apr 27;38(17):5538-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10220341 10220341]
-[[Category: Cytochrome-c peroxidase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Bhaskar B]]
-[[Category: Bhaskar, B.]]
+[[Category: Bonagura CA]]
-[[Category: Bonagura, C A.]]
+[[Category: Poulos TL]]
-[[Category: Poulos, T L.]]
+[[Category: Sundaramoorthy M]]
-[[Category: Sundaramoorthy, M.]]
-[[Category: helical bundle protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:11 2008''