1z21

<StructureSection load='1z21' size='340' side='right' caption='[[1z21]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1z21]] is a 1 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=1Z21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z21 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yscH, lcrP ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z21 OCA], [http://pdbe.org/1z21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z21 RCSB], [http://www.ebi.ac.uk/pdbsum/1z21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z21 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/YSCH_YERPE YSCH_YERPE]] Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function.

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== Publication Abstract from PubMed ==

Yersinia pestis, the causative agent of the plague, employs a type III secretion system (T3SS) to secrete and translocate virulence factors into to the cytoplasm of mammalian host cells. One of the secreted virulence factors is YopR. Little is known about the function of YopR other than that it is secreted into the extracellular milieu during the early stages of infection and that it contributes to virulence. Hoping to gain some insight into the function of YopR, we determined the crystal structure of its protease-resistant core domain, which consists of residues 38-149 out of 165 amino acids. The core domain is composed of five alpha-helices that display unexpected structural similarity with one domain of YopN, a central regulator of type III secretion in Y. pestis. This finding raises the possibility that YopR may play a role in the regulation of type III secretion.

Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR.,Schubot FD, Cherry S, Austin BP, Tropea JE, Waugh DS Protein Sci. 2005 Jun;14(6):1679-83. PMID:15930010<ref>PMID:15930010</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 1z21" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Austin, B P]]

[[Category: Cherry, S]]

[[Category: Schubot, F D]]

[[Category: Tropea, J E]]

[[Category: Waugh, D S]]

[[Category: Cell invasion]]

[[Category: Plague]]

[[Category: Type iii secretion]]

[[Category: Yopr]]