1hy5

<table><tr><td colspan='2'>[[1hy5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1HY5 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1he9|1he9]], [[1he1|1he1]], [[1g4u|1g4u]], [[1g4w|1g4w]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YOPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1hy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy5 OCA], [http://pdbe.org/1hy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hy5 RCSB], [http://www.ebi.ac.uk/pdbsum/1hy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/YOPE_YERPE YOPE_YERPE]] Essential virulence determinant; cytotoxic effector, involved in resistance to phagocytosis.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Yersinia pestis, the causative agent of bubonic plague, evades the immune response of the infected organism by using a type III (contact-dependent) secretion system to deliver effector proteins into the cytosol of mammalian cells, where they interfere with signaling pathways that regulate inflammation and cytoskeleton dynamics. The cytotoxic effector YopE functions as a potent GTPase-activating protein (GAP) for Rho family GTP-binding proteins, including RhoA, Rac1, and Cdc42. Down-regulation of these molecular switches results in the loss of cell motility and inhibition of phagocytosis, enabling Y. pestis to thrive on the surface of macrophages. We have determined the crystal structure of the GAP domain of YopE (YopE(GAP); residues 90-219) at 2.2-A resolution. Apart from the fact that it is composed almost entirely of alpha-helices, YopE(GAP) shows no obvious structural similarity with eukaryotic RhoGAP domains. Moreover, unlike the catalytically equivalent arginine fingers of the eukaryotic GAPs, which are invariably contained within flexible loops, the critical arginine in YopE(GAP) (Arg144) is part of an alpha-helix. The structure of YopE(GAP) is strikingly similar to the GAP domains from Pseudomonas aeruginosa (ExoS(GAP)) and Salmonella enterica (SptP(GAP)), despite the fact that the three amino acid sequences are not highly conserved. A comparison of the YopE(GAP) structure with those of the Rac1-ExoS(GAP) and Rac1-SptP complexes indicates that few, if any, significant conformational changes occur in YopE(GAP) when it interacts with its G protein targets. The structure of YopE(GAP) may provide an avenue for the development of novel therapeutic agents to combat plague.

Crystal structure of the Yersinia pestis GTPase activator YopE.,Evdokimov AG, Tropea JE, Routzahn KM, Waugh DS Protein Sci. 2002 Feb;11(2):401-8. PMID:11790850<ref>PMID:11790850</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1hy5" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Evdokimov, A G]]

[[Category: Routzahn, K M]]

[[Category: Tropea, J E]]

[[Category: Waugh, D S]]

[[Category: Arginine finger]]

[[Category: Toxin]]