1jya

<table><tr><td colspan='2'>[[1jya]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JYA 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">syce ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</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=1jya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jya OCA], [http://pdbe.org/1jya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jya RCSB], [http://www.ebi.ac.uk/pdbsum/1jya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jya ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/YERA_YERPE YERA_YERPE]] Positive regulator of YopE.

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== Publication Abstract from PubMed ==

In the type III secretory system of bacterial pathogens, a large number of sequence-divergent but characteristically small (approximately 14-19 kDa), acidic (pI approximately 4-5) chaperone proteins have been identified. We present the 1.74 A resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis. SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components. These patches are formed by structurally key residues that are conserved among many chaperones, suggesting shared structural and functional relationships. A negative electrostatic potential covers almost the entire surface of SycE and is likely conserved in character, but not in detail, among chaperones. The structure provides the first structural insights into possible modes of action of SycE and type III chaperones in general.

Structure of the Yersinia type III secretory system chaperone SycE.,Birtalan S, Ghosh P Nat Struct Biol. 2001 Nov;8(11):974-8. PMID:11685245<ref>PMID:11685245</ref>

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

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

== References ==

<references/>

[[Category: Birtalan, S]]

[[Category: Ghosh, P]]

[[Category: Chaperone]]

[[Category: Type iii secretion]]