1dcc
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dcc' size='340' side='right'caption='[[1dcc]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1dcc' size='340' side='right'caption='[[1dcc]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dcc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dcc]] 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=1DCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <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=OXY:OXYGEN+MOLECULE'>OXY</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=1dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcc OCA], [https://pdbe.org/1dcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcc RCSB], [https://www.ebi.ac.uk/pdbsum/1dcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcc ProSAT]</span></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=1dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcc OCA], [https://pdbe.org/1dcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcc RCSB], [https://www.ebi.ac.uk/pdbsum/1dcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1dcc ConSurf]. | </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=1dcc ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion. | ||
| - | |||
| - | 2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex.,Miller MA, Shaw A, Kraut J Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080<ref>PMID:7664080</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dcc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | *[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | ||
*[[Hemeproteins|Hemeproteins]] | *[[Hemeproteins|Hemeproteins]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
| - | [[Category: Cytochrome-c peroxidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kraut | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Miller | + | [[Category: Kraut J]] |
| - | [[Category: Shaw | + | [[Category: Miller MA]] |
| + | [[Category: Shaw A]] | ||
Current revision
2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX
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