1qf7

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{{Seed}}
 
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[[Image:1qf7.png|left|200px]]
 
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==STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1qf7", creates the "Structure Box" on the page.
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<StructureSection load='1qf7' size='340' side='right'caption='[[1qf7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qf7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QF7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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></td></tr>
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{{STRUCTURE_1qf7| PDB=1qf7 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qf7 OCA], [https://pdbe.org/1qf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qf7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qf7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qf7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qf7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional structures of two HPII variants, V169C and H392Q, have been determined at resolutions of 1.8 and 2.1 A, respectively. The V169C variant contains a new type of covalent bond between the sulfur atom of Cys(169) and a carbon atom on the imidazole ring of the essential His(128). This variant enzyme has only residual catalytic activity and contains heme b. The chain of water molecules visible in the main channel may reflect the organization of the hydrogen peroxide substrates in the active enzyme. Two alternative mechanisms, involving either compound I or free radical intermediates, are presented to explain the formation of the Cys-His covalent bond. The H392Q and H392E variants exhibit 75 and 25% of native catalytic activity, respectively. The Gln(392) variant contains only heme b, whereas the Glu(392) variant contains a mixture of heme b and cis and trans isomers of heme d, suggesting of a role for this residue in heme conversion. Replacement of either Gln(419) and Ser(414), both of which interact with the heme, affected the cis:trans ratio of spirolactone heme d. Implications for the heme oxidation mechanism and the His-Tyr bond formation in HPII are considered.
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===STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI===
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Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli.,Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I J Biol Chem. 1999 Sep 24;274(39):27717-25. PMID:10488114<ref>PMID:10488114</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qf7" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10488114}}, adds the Publication Abstract to the page
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*[[Catalase 3D structures|Catalase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10488114 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10488114}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1QF7 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF7 OCA].
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==Reference==
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<ref group="xtra">PMID:10488114</ref><references group="xtra"/>
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[[Category: Catalase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Fita, I.]]
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[[Category: Large Structures]]
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[[Category: Loewen, P C.]]
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[[Category: Fita I]]
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[[Category: Mate, M J.]]
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[[Category: Loewen PC]]
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[[Category: Covalent modification]]
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[[Category: Mate MJ]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:34:22 2009''
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Current revision

STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI

PDB ID 1qf7

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