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New page: ==Crystal structure of native catalase-peroxidase KatG at pH8.0== <StructureSection load='5sw4' size='340' side='right' caption='5sw4, resolution 1.90Å' scene=''>... |
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==Crystal structure of native catalase-peroxidase KatG at pH8.0== | ==Crystal structure of native catalase-peroxidase KatG at pH8.0== | ||
<StructureSection load='5sw4' size='340' side='right' caption='[[5sw4]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5sw4' size='340' side='right'caption='[[5sw4]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5sw4]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2b2o 2b2o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SW4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5sw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2b2o 2b2o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SW4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TOX:1-HYDROPEROXY-L-TRYPTOPHAN'>TOX</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5sw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sw4 OCA], [https://pdbe.org/5sw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sw4 RCSB], [https://www.ebi.ac.uk/pdbsum/5sw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sw4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KATG_BURP1 KATG_BURP1] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5sw4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5sw4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Catalase 3D structures|Catalase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Burkholderia pseudomallei 1710b]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Loewen PC]] | ||
Latest revision as of 15:48, 4 October 2023
Crystal structure of native catalase-peroxidase KatG at pH8.0Crystal structure of native catalase-peroxidase KatG at pH8.0
Structural highlights
FunctionKATG_BURP1 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Publication Abstract from PubMedThe catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp. A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.,Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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