View source for 2bsj


==Native Crystal Structure of the Type III Secretion chaperone SycT from Yersinia enterocolitica==
<StructureSection load='2bsj' size='340' side='right'caption='[[2bsj]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsj OCA], [https://pdbe.org/2bsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsj RCSB], [https://www.ebi.ac.uk/pdbsum/2bsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYCT_YEREN SYCT_YEREN] Functions as a specific chaperone for YopT.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic Yersinia species use a type III secretion (TTS) system to deliver a number of cytotoxic effector proteins directly into the mammalian host cell. To ensure effective translocation, several such effector proteins transiently bind to specific chaperones in the bacterial cytoplasm. Correspondingly, SycT is the chaperone of YopT, a cysteine protease that cleaves the membrane-anchor of Rho-GTPases in the host. We have analyzed the complex between YopT and SycT and determined the structure of SycT in three crystal forms. Biochemical studies indicate a stoichometric effector/chaperone ratio of 1:2 and the chaperone-binding site contains at least residues 52-103 of YopT. The crystal structures reveal a SycT homodimer with an overall fold similar to that of other TTS effector chaperones. In contrast to the canonical five-stranded anti-parallel beta-sheet flanked by three alpha-helices, SycT lacks the dimerization alpha-helix and has an additional beta-strand capable of undergoing a conformational change. The dimer interface consists of two beta-strands and the connecting loops. Two hydrophobic patches involved in effector binding in other TTS effector chaperones are also found in SycT. The structural similarity of SycT to other chaperones and the spatial conservation of effector-binding sites support the idea that TTS effector chaperones form a single functional and structural group.

Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT.,Buttner CR, Cornelis GR, Heinz DW, Niemann HH Protein Sci. 2005 Aug;14(8):1993-2002. PMID:16046625<ref>PMID:16046625</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2bsj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia enterocolitica]]
[[Category: Buttner CR]]
[[Category: Cornelis GR]]
[[Category: Heinz DW]]
[[Category: Niemann HH]]