1zof
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= tsaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | |GENE= tsaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zof OCA], [http://www.ebi.ac.uk/pdbsum/1zof PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zof RCSB]</span> | ||
}} | }} | ||
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[[Category: toroide-shaped complex]] | [[Category: toroide-shaped complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:39:31 2008'' |
Revision as of 22:39, 30 March 2008
| |||||||
| , resolution 2.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | tsaA (Helicobacter pylori) | ||||||
| Activity: | Peroxiredoxin, with EC number 1.11.1.15 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori
Overview
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
1ZOF is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
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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