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| | ==Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942== | | ==Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942== |
| - | <StructureSection load='3x16' size='340' side='right' caption='[[3x16]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='3x16' size='340' side='right'caption='[[3x16]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3x16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3X16 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3x16]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X16 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEB:HEME+B/C'>HEB</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wnu|3wnu]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEB:HEME+B/C'>HEB</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">katG, Synpcc7942_1656 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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=3x16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x16 OCA], [https://pdbe.org/3x16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x16 RCSB], [https://www.ebi.ac.uk/pdbsum/3x16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x16 ProSAT]</span></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=3x16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x16 OCA], [http://pdbe.org/3x16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x16 RCSB], [http://www.ebi.ac.uk/pdbsum/3x16 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3x16 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KATG_SYNE7 KATG_SYNE7]] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.[HAMAP-Rule:MF_01961] | + | [https://www.uniprot.org/uniprot/KATG_SYNE7 KATG_SYNE7] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.[HAMAP-Rule:MF_01961] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3x16" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3x16" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Catalase 3D structures|Catalase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anacystis nidulans r2]] | + | [[Category: Large Structures]] |
| - | [[Category: Catalase peroxidase]] | + | [[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] |
| - | [[Category: Kamachi, S]] | + | [[Category: Kamachi S]] |
| - | [[Category: Tada, T]] | + | [[Category: Tada T]] |
| - | [[Category: Wada, K]] | + | [[Category: Wada K]] |
| - | [[Category: Catalase subfamily]]
| + | |
| - | [[Category: Cross-link]]
| + | |
| - | [[Category: Heme b fe]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Trp-tyr-met adduct]]
| + | |
| Structural highlights
Function
KATG_SYNE7 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.[HAMAP-Rule:MF_01961]
Publication Abstract from PubMed
Isoniazid (INH) is a pro-drug that has been extensively used to treat tuberculosis. INH is activated by the heme enzyme catalase-peroxidase (KatG), but the mechanism of the activation is poorly understood, in part because the INH binding site has not been clearly established. Here, we observed that a single-residue mutation of KatG from Synechococcus elongatus PCC7942 (SeKatG), W78F, enhances INH activation. The crystal structure of INH-bound KatG-W78F revealed that INH binds to the heme pocket. The results of a thermal-shift assay implied that the flexibility of the SeKatG molecule is increased by the W78F mutation, allowing the INH molecule to easily invade the heme pocket through the access channel on the gamma-edge side of the heme.
Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazid.,Kamachi S, Hirabayashi K, Tamoi M, Shigeoka S, Tada T, Wada K FEBS Lett. 2015 Jan 2;589(1):131-7. doi: 10.1016/j.febslet.2014.11.037. Epub 2014, Dec 3. PMID:25479089[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kamachi S, Hirabayashi K, Tamoi M, Shigeoka S, Tada T, Wada K. Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazid. FEBS Lett. 2015 Jan 2;589(1):131-7. doi: 10.1016/j.febslet.2014.11.037. Epub 2014, Dec 3. PMID:25479089 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.037
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