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New page: left|200px<br /><applet load="1zof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zof, resolution 2.95Å" /> '''Crystal structure of... |
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== | ==Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori== | ||
The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl | <StructureSection load='1zof' size='340' side='right'caption='[[1zof]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zof]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOF 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]] 2.95Å</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=1zof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zof OCA], [https://pdbe.org/1zof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zof RCSB], [https://www.ebi.ac.uk/pdbsum/1zof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zof ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AHPC_HELPJ AHPC_HELPJ] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[UniProtKB:P0A251] | |||
== 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/zo/1zof_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1zof ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl hydroperoxide-reductase, is a member of the ubiquitous 2-Cys peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant enzymes. Prxs exert the protective antioxidant role in cells through their peroxidase activity, whereby hydrogen peroxide, peroxynitrite and a wide range of organic hydroperoxides (ROOH) are reduced and detoxified (ROOH + 2e(-)-->ROH + H2O). In this study AhpC has been cloned and overexpressed in E. coli. After purification to homogeneity, crystals of the recombinant protein were grown. They diffract to 2.95 A resolution using synchrotron radiation. The crystal structure of AhpC has been determined using the molecular replacement method (R = 23.6%, R(free) = 25.9%). The model, similar in the overall to other members of the 2-Cys Prx family crystallized as toroide-shaped complexes, consists of a pentameric arrangement of homodimers [(alpha2)5 decamer]. The model of AhpC from H. pylori presents significant differences with respect to other members of the family: apart from some loop regions, alpha5-helix and the C-terminus is shifted, preventing the C-terminal tail of the second subunit from extending toward this region of the molecule. Oligomerization properties of AhpC have been also characterized by gel filtration chromatography. | |||
Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori.,Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G Biochim Biophys Acta. 2005 Dec 1;1753(2):240-6. Epub 2005 Sep 21. PMID:16213196<ref>PMID:16213196</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zof" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Battistutta R]] | |||
[[Category: Battistutta | [[Category: Cendron L]] | ||
[[Category: Cendron | [[Category: Kelleher D]] | ||
[[Category: Kelleher | [[Category: Papinutto E]] | ||
[[Category: Papinutto | [[Category: Windle HJ]] | ||
[[Category: Windle | [[Category: Zanotti G]] | ||
[[Category: Zanotti | |||
Latest revision as of 10:46, 30 October 2024
Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter PyloriCrystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori
Structural highlights
FunctionAHPC_HELPJ Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[UniProtKB:P0A251] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl hydroperoxide-reductase, is a member of the ubiquitous 2-Cys peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant enzymes. Prxs exert the protective antioxidant role in cells through their peroxidase activity, whereby hydrogen peroxide, peroxynitrite and a wide range of organic hydroperoxides (ROOH) are reduced and detoxified (ROOH + 2e(-)-->ROH + H2O). In this study AhpC has been cloned and overexpressed in E. coli. After purification to homogeneity, crystals of the recombinant protein were grown. They diffract to 2.95 A resolution using synchrotron radiation. The crystal structure of AhpC has been determined using the molecular replacement method (R = 23.6%, R(free) = 25.9%). The model, similar in the overall to other members of the 2-Cys Prx family crystallized as toroide-shaped complexes, consists of a pentameric arrangement of homodimers [(alpha2)5 decamer]. The model of AhpC from H. pylori presents significant differences with respect to other members of the family: apart from some loop regions, alpha5-helix and the C-terminus is shifted, preventing the C-terminal tail of the second subunit from extending toward this region of the molecule. Oligomerization properties of AhpC have been also characterized by gel filtration chromatography. Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori.,Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G Biochim Biophys Acta. 2005 Dec 1;1753(2):240-6. Epub 2005 Sep 21. PMID:16213196[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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