1he9: Difference between revisions

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[[Image:1he9.~~gif~~|left|200px]]

[[Image:1he9.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN~~'''~~

===CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN===

~~==Overview==~~

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~~Pseudomonas aeruginosa is an opportunistic bacterial pathogen of great medical relevance. One of its major toxins~~, ~~exoenzyme S (ExoS)~~, ~~is a dual function protein with a C-terminal Ras-ADP-ribosylation domain and an N-terminal GTPase activating protein (GAP) domain specific for Rho-family proteins. We report here~~ the ~~three-dimensional structure of~~ the ~~N-terminal domain of ExoS determined by X-ray crystallography to 2~~.~~4 A resolution~~. ~~Its fold~~ is ~~all helical with a four helix bundle core capped by additional irregular helices~~. ~~Loops that are known to interact with Rho~~-~~family proteins show very large mobility. Considering the importance of ExoS in Pseudomonas pathogenicity, this structure could be of interest for drug targeting.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11226412}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11226412 is the PubMed ID number.

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==About this Structure==

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[[Category: Toxin]]

[[Category: Virulence factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:45:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:04:01 2008''

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-[[Image:1he9.gif|left|200px]]
+{{Seed}}
+[[Image:1he9.png|left|200px]]
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 {{STRUCTURE_1he9|  PDB=1he9  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN'''
+===CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA EXOS TOXIN===
-==Overview==
+<!--
-Pseudomonas aeruginosa is an opportunistic bacterial pathogen of great medical relevance. One of its major toxins, exoenzyme S (ExoS), is a dual function protein with a C-terminal Ras-ADP-ribosylation domain and an N-terminal GTPase activating protein (GAP) domain specific for Rho-family proteins. We report here the three-dimensional structure of the N-terminal domain of ExoS determined by X-ray crystallography to 2.4 A resolution. Its fold is all helical with a four helix bundle core capped by additional irregular helices. Loops that are known to interact with Rho-family proteins show very large mobility. Considering the importance of ExoS in Pseudomonas pathogenicity, this structure could be of interest for drug targeting.
+The line below this paragraph, {{ABSTRACT_PUBMED_11226412}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11226412 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11226412}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Toxin]]
 [[Category: Virulence factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:45:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:04:01 2008''