1ttw

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[[Image:1ttw.png|left|200px]]
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==Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2==
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<StructureSection load='1ttw' size='340' side='right' caption='[[1ttw]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ttw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TTW FirstGlance]. <br>
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</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=1ttw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ttw RCSB], [http://www.ebi.ac.uk/pdbsum/1ttw PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pathogenic Yersinia species use a type III secretion system to inject cytotoxic effector proteins directly into the cytosol of mammalian cells, where they neutralize the innate immune response by interfering with the signal-transduction pathways that control phagocytosis and inflammation. To be exported efficiently, some effectors must transiently associate with cognate cytoplasmic secretion chaperones. SycH is the chaperone for YopH, a potent eukaryotic-like protein tyrosine phosphatase that is essential for virulence. SycH also binds two negative regulators of type III secretion, YscM1 and YscM2, both of which share significant sequence homology with the chaperone-binding domain of YopH. Here, the structure of a complex between SycH and a stable fragment of YscM2 that was designed on the basis of limited proteolysis experiments is presented. The overall fold of SycH is very similar to the structures of other homodimeric secretion chaperones that have been determined to date. YscM2 wraps around SycH in an extended fashion, with some secondary but no tertiary structure, assuming a conformation distinct from the globular fold that it is predicted to adopt in the absence of SycH.
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{{STRUCTURE_1ttw| PDB=1ttw | SCENE= }}
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Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2.,Phan J, Tropea JE, Waugh DS Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1591-9. Epub 2004, Aug 26. PMID:15333930<ref>PMID:15333930</ref>
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===Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15333930}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1ttw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTW OCA].
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</StructureSection>
[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
[[Category: Phan, J.]]
[[Category: Phan, J.]]

Revision as of 08:35, 8 October 2014

Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2

1ttw, resolution 2.38Å

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