3pq3: Difference between revisions
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==Structure of I274C variant of E. coli KatE[] - Images 7-12== | ==Structure of I274C variant of E. coli KatE[] - Images 7-12== | ||
<StructureSection load='3pq3' size='340' side='right' caption='[[3pq3]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='3pq3' size='340' side='right' caption='[[3pq3]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pq3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3pq3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PQ3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9p|3p9p]], [[3p9q|3p9q]], [[3p9r|3p9r]], [[3p9s|3p9s]], [[3pq2|3pq2]], [[3pq4|3pq4]], [[3pq5|3pq5]], [[3pq6|3pq6]], [[3pq7|3pq7]], [[3pq8|3pq8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9p|3p9p]], [[3p9q|3p9q]], [[3p9r|3p9r]], [[3p9s|3p9s]], [[3pq2|3pq2]], [[3pq4|3pq4]], [[3pq5|3pq5]], [[3pq6|3pq6]], [[3pq7|3pq7]], [[3pq8|3pq8]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1732, JW1721, katE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1732, JW1721, katE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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 Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=3pq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pq3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pq3 RCSB], [http://www.ebi.ac.uk/pdbsum/3pq3 PDBsum]</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=3pq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pq3 OCA], [http://pdbe.org/3pq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pq3 RCSB], [http://www.ebi.ac.uk/pdbsum/3pq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pq3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3pq3" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Catalase]] | [[Category: Catalase]] | ||
[[Category: | [[Category: Ecoli]] | ||
[[Category: Carpena, X]] | [[Category: Carpena, X]] | ||
[[Category: Chelikani, P]] | [[Category: Chelikani, P]] | ||
Revision as of 05:03, 5 August 2016
Structure of I274C variant of E. coli KatE[] - Images 7-12Structure of I274C variant of E. coli KatE[] - Images 7-12
Structural highlights
Function[CATE_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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