1zof: Difference between revisions
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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[[Image:1zof.gif|left|200px]]<br /><applet load="1zof" size=" | [[Image:1zof.gif|left|200px]]<br /><applet load="1zof" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1zof, resolution 2.95Å" /> | caption="1zof, resolution 2.95Å" /> | ||
'''Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori'''<br /> | '''Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori'''<br /> | ||
==Overview== | ==Overview== | ||
The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl | 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. | ||
==About this Structure== | ==About this Structure== | ||
1ZOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] Full crystallographic information is available from [http:// | 1ZOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kelleher, D.]] | [[Category: Kelleher, D.]] | ||
[[Category: Papinutto, E.]] | [[Category: Papinutto, E.]] | ||
[[Category: Windle, H | [[Category: Windle, H J.]] | ||
[[Category: Zanotti, G.]] | [[Category: Zanotti, G.]] | ||
[[Category: decamer]] | [[Category: decamer]] | ||
[[Category: toroide-shaped complex]] | [[Category: toroide-shaped complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:33 2008'' | ||
Revision as of 17:17, 21 February 2008
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Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori
OverviewOverview
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.
About this StructureAbout this Structure
1ZOF is a Single protein structure of sequence from Helicobacter pylori. Active as Peroxiredoxin, with EC number 1.11.1.15 Full crystallographic information is available from OCA.
ReferenceReference
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
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