2v5g: Difference between revisions

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-{{Seed}}
-[[Image:2v5g.png|left|200px]]
-<!--
+==Crystal structure of the mutated N263A YscU C-terminal domain==
-The line below this paragraph, containing "STRUCTURE_2v5g", creates the "Structure Box" on the page.
+<StructureSection load='2v5g' size='340' side='right'caption='[[2v5g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2v5g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5G FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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>
-{{STRUCTURE_2v5g|  PDB=2v5g  |  SCENE=  }}
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2w0r|2w0r]]</div></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=2v5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5g OCA], [https://pdbe.org/2v5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5g RCSB], [https://www.ebi.ac.uk/pdbsum/2v5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5g ProSAT]</span></td></tr>
+</table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/2v5g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2v5g ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The inner-membrane protein YscU has an important role during the assembly of the Yersinia enterocolitica type III secretion injectisome. Its cytoplasmic domain (YscU(C)) recognizes translocators as individual substrates in the export hierarchy. Activation of YscU entails autocleavage at a conserved NPTH motif. Modification of this motif markedly changes the properties of YscU, including translocator export cessation and production of longer injectisome needles. We determined the crystal structures of the uncleaved variants N263A and N263D of YscU(C) at 2.05 A and 1.55 A resolution, respectively. The globular domain is found to consist of a central, mixed beta-sheet surrounded by alpha-helices. The NPTH motif forms a type II beta-turn connecting two beta-strands. NMR analysis of cleaved and uncleaved YscU(C) indicates that the global structure of the protein is retained in cleaved YscU(C). The structure of YscU(C) variant N263D reveals that wild type YscU(C) is poised for cleavage due to an optimal reaction geometry for nucleophilic attack of the scissile bond by the side chain of Asn263. In vivo analysis of N263Q and H266A/R314A YscU variants showed a phenotype that combines the absence of translocator secretion with normal needle-length control. Comparing the structure of YscU to those of related proteins reveals that the linker domain between the N-terminal transmembrane domain and the autocleavage domain can switch from an extended to a largely alpha-helical conformation, allowing for optimal positioning of the autocleavage domain during injectisome assembly.
-===CRYSTAL STRUCTURE OF THE MUTATED N263A YSCU C-TERMINAL DOMAIN===
+Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica.,Wiesand U, Sorg I, Amstutz M, Wagner S, van den Heuvel J, Luhrs T, Cornelis GR, Heinz DW J Mol Biol. 2009 Jan 23;385(3):854-66. Epub 2008 Oct 19. PMID:18976663<ref>PMID:18976663</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_18976663}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2v5g" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18976663 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18976663}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
-V5G is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5G OCA].
+[[Category: Large Structures]]
+[[Category: Amstutz, M]]
-==Reference==
+[[Category: Cornelis, G R]]
-<ref group="xtra">PMID:18976663</ref><ref group="xtra">PMID:8045883</ref><references group="xtra"/>
+[[Category: Heinz, D W]]
-[[Category: Yersinia enterocolitica]]
+[[Category: Heuvel, J Van Den]]
-[[Category: Amstutz, M.]]
+[[Category: Luehrs, T]]
-[[Category: Cornelis, G R.]]
+[[Category: Sorg, I]]
-[[Category: Heinz, D W.]]
+[[Category: Wagner, S]]
-[[Category: Heuvel, J Van Den.]]
+[[Category: Wiesand, U]]
-[[Category: Luehrs, T.]]
-[[Category: Sorg, I.]]
-[[Category: Wagner, S.]]
-[[Category: Wiesand, U.]]
 [[Category: Autocleavage]]
 [[Category: Membrane protein]]
@@ Line 38: / Line 47: @@
 [[Category: Recognition protein]]
 [[Category: Type iii secretion system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 21 09:37:08 2009''