1ttw
From Proteopedia
(New page: 200px<br /><applet load="1ttw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ttw, resolution 2.38Å" /> '''Crystal structure of...) |
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| - | [[Image:1ttw.gif|left|200px]]<br /><applet load="1ttw" size=" | + | [[Image:1ttw.gif|left|200px]]<br /><applet load="1ttw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ttw, resolution 2.38Å" /> | caption="1ttw, resolution 2.38Å" /> | ||
'''Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2'''<br /> | '''Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pathogenic Yersinia species use a type III secretion system to inject | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TTW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis_co92 Yersinia pestis co92]. Full crystallographic information is available from [http:// | + | 1TTW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis_co92 Yersinia pestis co92]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Yersinia pestis co92]] | [[Category: Yersinia pestis co92]] | ||
[[Category: Phan, J.]] | [[Category: Phan, J.]] | ||
| - | [[Category: Tropea, J | + | [[Category: Tropea, J E.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: type iii secretion]] | [[Category: type iii secretion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:25 2008'' |
Revision as of 13:17, 21 February 2008
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Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2
Overview
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.
About this Structure
1TTW is a Protein complex structure of sequences from Yersinia pestis co92. Full crystallographic information is available from OCA.
Reference
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
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