3cei: Difference between revisions

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[[Image:3cei.~~jpg~~|left|200px]]

[[Image:3cei.png|left|200px]]

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~~'''~~Crystal Structure of Superoxide Dismutase from Helicobacter pylori~~'''~~

===Crystal Structure of Superoxide Dismutase from Helicobacter pylori===

~~==Overview==~~

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~~Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron.~~ The ~~structure of~~ this ~~antioxidant protein has been determined~~ at 2.~~4 A resolution~~. It is ~~a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with~~ the ~~corresponding enzyme from Escherichia coli~~. ~~The model is compared with those of other dimeric Fe~~-~~containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C~~-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve.

The line below this paragraph, {{ABSTRACT_PUBMED_18502213}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18502213 is the PubMed ID number.

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==About this Structure==

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[[Category: Zanotti, G.]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jun~~ 11 10:49:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:39:27 2008''

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-[[Image:3cei.jpg|left|200px]]
+{{Seed}}
+[[Image:3cei.png|left|200px]]
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 {{STRUCTURE_3cei|  PDB=3cei  |  SCENE=  }}
-'''Crystal Structure of Superoxide Dismutase from Helicobacter pylori'''
+===Crystal Structure of Superoxide Dismutase from Helicobacter pylori===
-==Overview==
+<!--
-Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron. The structure of this antioxidant protein has been determined at 2.4 A resolution. It is a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with the corresponding enzyme from Escherichia coli. The model is compared with those of other dimeric Fe-containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve.
+The line below this paragraph, {{ABSTRACT_PUBMED_18502213}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18502213 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18502213}}
 ==About this Structure==
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 [[Category: Zanotti, G.]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:49:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:39:27 2008''