1he9: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Crystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxin==
-<StructureSection load='1he9' size='340' side='right' caption='[[1he9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1he9' size='340' side='right'caption='[[1he9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1he9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HE9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1he9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HE9 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1he1|1he1]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXOS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1he9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1he9 OCA], [https://pdbe.org/1he9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1he9 RCSB], [https://www.ebi.ac.uk/pdbsum/1he9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1he9 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1he9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1he9 OCA], [http://pdbe.org/1he9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1he9 RCSB], [http://www.ebi.ac.uk/pdbsum/1he9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1he9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q51451_PSEAI Q51451_PSEAI]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1he9 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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<ref>PMID:11226412</ref>
+==See Also==
+*[[Exoenzyme 3D structures|Exoenzyme 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1he9" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Barbieri, J T]]
+[[Category: Large Structures]]
-[[Category: Renault, L]]
-[[Category: Wittinghofer, A]]
-[[Category: Wolf, E]]
-[[Category: Wurtele, M]]
-[[Category: Exo]]
-[[Category: Gap]]
 [[Category: Pseudomonas aeruginosa]]
-[[Category: Signal transduction]]
+[[Category: Barbieri JT]]
-[[Category: Toxin]]
+[[Category: Renault L]]
-[[Category: Virulence factor]]
+[[Category: Wittinghofer A]]
+[[Category: Wolf E]]
+[[Category: Wurtele M]]