1ye9
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1ye9.png|left|200px]] | ||
- | < | + | ==Crystal structure of proteolytically truncated catalase HPII from E. coli== |
- | + | <StructureSection load='1ye9' size='340' side='right'caption='[[1ye9]], [[Resolution|resolution]] 2.80Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1ye9]] is a 16 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=1YE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YE9 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</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=1ye9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ye9 OCA], [https://pdbe.org/1ye9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ye9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ye9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ye9 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == 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. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ye/1ye9_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1ye9 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The large subunit catalase HPII from Escherichia coli can be truncated by proteolysis to a structure similar to small subunit catalases. Mass spectrometry analysis indicates that there is some heterogeneity in the precise cleavage sites, but approximately 74 N-terminal residues, 189 C-terminal residues, and a 9-11-residue internal fragment, including residues 298-308, are removed. Crystal structure refinement at 2.8 A reveals that the tertiary and quaternary structure of the native enzyme is retained with only very subtle changes despite the loss of 36% of the sequence. The truncated variant exhibits a 1.8 times faster turnover rate and enhanced sensitivity to high concentrations of H(2)O(2), consistent with easier access of the substrate to the active site. In addition, the truncated variant is more sensitive to inhibition, particularly by reagents such as aminotriazole and azide which are larger than substrate H(2)O(2). The main channel leading to the heme cavity is largely unaffected by the truncation, but the lateral channel is shortened and its entrance widened by removal of the C-terminal domain, providing an explanation for easier access to the active site. Opening of the entrance to the lateral channel also opens the putative NADPH binding site, but NADPH binding could not be demonstrated. Despite the lack of bound NADPH, the compound I species of both native and truncated HPII are reduced back to the resting state with compound II being evident in the absorbance spectrum only of the heme b-containing H392A variant. | ||
- | + | Characterization of a large subunit catalase truncated by proteolytic cleavage.,Chelikani P, Carpena X, Perez-Luque R, Donald LJ, Duckworth HW, Switala J, Fita I, Loewen PC Biochemistry. 2005 Apr 19;44(15):5597-605. PMID:15823018<ref>PMID:15823018</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1ye9" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Catalase 3D structures|Catalase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Carpena | + | [[Category: Carpena X]] |
- | [[Category: Chelikani | + | [[Category: Chelikani P]] |
- | [[Category: Donald | + | [[Category: Donald LJ]] |
- | [[Category: Duckworth | + | [[Category: Duckworth HW]] |
- | [[Category: Fita | + | [[Category: Fita I]] |
- | [[Category: Loewen | + | [[Category: Loewen PC]] |
- | [[Category: Perez-Luque | + | [[Category: Perez-Luque R]] |
- | [[Category: Switala | + | [[Category: Switala J]] |
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Current revision
Crystal structure of proteolytically truncated catalase HPII from E. coli
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