1s2x: Difference between revisions

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~~'''~~Crystal structure of Cag-Z from Helicobacter pylori~~'''~~

===Crystal structure of Cag-Z from Helicobacter pylori===

~~==Overview==~~

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~~CagZ~~, ~~a 23 kDa protein encoded by~~ the ~~cagZ gene~~ (~~HP0526~~) ~~of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed~~, ~~purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of~~ the ~~total residues~~. ~~Three~~-~~dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C~~-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.

The line below this paragraph, {{ABSTRACT_PUBMED_15223328}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15223328 is the PubMed ID number.

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==About this Structure==

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[[Category: Helicobacter pylori]]

[[Category: Type iv secretion system]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3~~ 08:~~13:47~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:08:12 2008''

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-[[Image:1s2x.jpg|left|200px]]
+{{Seed}}
+[[Image:1s2x.png|left|200px]]
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 {{STRUCTURE_1s2x|  PDB=1s2x  |  SCENE=  }}
-'''Crystal structure of Cag-Z from Helicobacter pylori'''
+===Crystal structure of Cag-Z from Helicobacter pylori===
-==Overview==
+<!--
-CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.
+The line below this paragraph, {{ABSTRACT_PUBMED_15223328}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15223328 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15223328}}
 ==About this Structure==
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 [[Category: Helicobacter pylori]]
 [[Category: Type iv secretion system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:13:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:08:12 2008''