5sw4: Difference between revisions

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<StructureSection load='5sw4' size='340' side='right'caption='[[5sw4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5sw4' size='340' side='right'caption='[[5sw4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5sw4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burp1 Burp1]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SW4 FirstGlance]. <br>
<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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TOX:1-HYDROPEROXY-L-TRYPTOPHAN'>TOX</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5l02|5l02]], [[5l05|5l05]], [[5sw5|5sw5]], [[5sw6|5sw6]], [[5sx0|5sx0]], [[5sx1|5sx1]], [[5sx2|5sx2]], [[5sx3|5sx3]], [[5sx6|5sx6]], [[5sx7|5sx7]], [[5sxq|5sxq]], [[5sxr|5sxr]], [[5sxs|5sxs]], [[5sxt|5sxt]], [[5sxx|5sxx]], [[5syh|5syh]], [[5syi|5syi]], [[5syj|5syj]], [[5syk|5syk]], [[5syl|5syl]], [[5syu|5syu]], [[5syv|5syv]], [[5syw|5syw]], [[5syx|5syx]], [[5syy|5syy]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">katG, BURPS1710b_3366 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase_peroxidase Catalase peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.21 1.11.1.21] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5sw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sw4 OCA], [http://pdbe.org/5sw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5sw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sw4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KATG_BURP1 KATG_BURP1]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.  
[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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Burp1]]
[[Category: Burkholderia pseudomallei 1710b]]
[[Category: Catalase peroxidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Loewen, P C]]
[[Category: Loewen PC]]
[[Category: Catalase]]
[[Category: Molecular switch]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Ph change]]

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

5sw4 is a 2 chain structure with sequence from Burkholderia pseudomallei 1710b. This structure supersedes the now removed PDB entry 2b2o. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KATG_BURP1 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.

Publication Abstract from PubMed

The 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 Also

References

  1. ↑ Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC. A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases. EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084

5sw4, resolution 1.90Å

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