1he9

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(New page: 200px<br /><applet load="1he9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1he9, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 00:21, 25 November 2007

Image:1he9.gif

1he9, resolution 2.40Å

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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.

About this Structure

1HE9 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Structure of the ExoS GTPase activating domain., Wurtele M, Renault L, Barbieri JT, Wittinghofer A, Wolf E, FEBS Lett. 2001 Feb 23;491(1-2):26-9. PMID:11226412

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