2bsj
From Proteopedia
(New page: 200px<br /><applet load="2bsj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bsj, resolution 1.83Å" /> '''NATIVE CRYSTAL STRUC...) |
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| - | [[Image:2bsj.gif|left|200px]]<br /><applet load="2bsj" size=" | + | [[Image:2bsj.gif|left|200px]]<br /><applet load="2bsj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bsj, resolution 1.83Å" /> | caption="2bsj, resolution 1.83Å" /> | ||
'''NATIVE CRYSTAL STRUCTURE OF THE TYPE III SECRETION CHAPERONE SYCT FROM YERSINIA ENTEROCOLITICA'''<br /> | '''NATIVE CRYSTAL STRUCTURE OF THE TYPE III SECRETION CHAPERONE SYCT FROM YERSINIA ENTEROCOLITICA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pathogenic Yersinia species use a type III secretion (TTS) system to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2BSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2BSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia enterocolitica]] | [[Category: Yersinia enterocolitica]] | ||
| - | [[Category: Buttner, C | + | [[Category: Buttner, C R.]] |
| - | [[Category: Cornelis, G | + | [[Category: Cornelis, G R.]] |
| - | [[Category: Heinz, D | + | [[Category: Heinz, D W.]] |
| - | [[Category: Niemann, H | + | [[Category: Niemann, H H.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
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[[Category: yopt]] | [[Category: yopt]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:11 2008'' |
Revision as of 14:41, 21 February 2008
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NATIVE CRYSTAL STRUCTURE OF THE TYPE III SECRETION CHAPERONE SYCT FROM YERSINIA ENTEROCOLITICA
Overview
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.
About this Structure
2BSJ is a Single protein structure of sequence from Yersinia enterocolitica with as ligand. Full crystallographic information is available from OCA.
Reference
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
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