3pq5: Difference between revisions
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<StructureSection load='3pq5' size='340' side='right'caption='[[3pq5]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3pq5' size='340' side='right'caption='[[3pq5]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pq5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3pq5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PQ5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HDE:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE+17R,+18S'>HDE</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HDE:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE+17R,+18S'>HDE</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=3pq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pq5 OCA], [https://pdbe.org/3pq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pq5 RCSB], [https://www.ebi.ac.uk/pdbsum/3pq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pq5 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=3pq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pq5 OCA], [https://pdbe.org/3pq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pq5 RCSB], [https://www.ebi.ac.uk/pdbsum/3pq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pq5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CATE_ECOLI CATE_ECOLI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. | |||
<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: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Carpena | [[Category: Carpena X]] | ||
[[Category: Chelikani | [[Category: Chelikani P]] | ||
[[Category: Fita | [[Category: Fita I]] | ||
[[Category: Jha | [[Category: Jha V]] | ||
[[Category: Loewen | [[Category: Loewen PC]] | ||
[[Category: Louis | [[Category: Louis S]] | ||
Latest revision as of 12:59, 6 September 2023
Structure of I274C variant of E. coli KatE[] - Images 19-24Structure of I274C variant of E. coli KatE[] - Images 19-24
Structural highlights
FunctionCATE_ECOLI Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Publication Abstract from PubMedHeme-containing catalases have been extensively studied, revealing the roles of many residues, the existence of two heme orientations, flipped 180 degrees relative to one another along the propionate-vinyl axis, and the presence of both heme b and heme d. The focus of this report is a residue, situated adjacent to the vinyl groups of the heme at the entrance of the lateral channel, with an unusual main chain geometry that is conserved in all catalase structures so far determined. In Escherichia coli catalase HPII, the residue is Ile274, and replacing it with Gly, Ala, and Val, found at the same location in other catalases, results in a reduction in catalytic efficiency, a reduced intensity of the Soret absorbance band, and a mixture of heme orientations and species. The reduced turnover rates and higher H(2)O(2) concentrations required to attain equivalent reaction velocities are explained in terms of less efficient containment of substrate H(2)O(2) in the heme cavity arising from easier escape through the more open entrance to the lateral channel created by the smaller side chains of Gly and Ala. Inserting a Cys at position 274 resulted in the heme being covalently linked to the protein through a Cys-vinyl bond that is hypersensitive to X-ray irradiation being largely degraded within seconds of exposure to the X-ray beam. Two heme orientations, flipped along the propionate-vinyl axis, are found in the Ala, Val, and Cys variants. Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli.,Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC Biochemistry. 2011 Mar 29;50(12):2101-10. Epub 2011 Mar 3. PMID:21332158[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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