2bho
From Proteopedia
(New page: 200px<br /><applet load="2bho" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bho, resolution 2.60Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2bho.gif|left|200px]]<br /><applet load="2bho" size=" | + | [[Image:2bho.gif|left|200px]]<br /><applet load="2bho" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bho, resolution 2.60Å" /> | caption="2bho, resolution 2.60Å" /> | ||
'''CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION CHAPERONE SYCT'''<br /> | '''CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION CHAPERONE SYCT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Several Gram-negative pathogens deploy type III secretion systems (TTSSs) | + | Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 angstroms resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT(C139S) is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT. |
==About this Structure== | ==About this Structure== | ||
| - | 2BHO 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 PT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2BHO 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=PT:'>PT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: yersinia]] | [[Category: yersinia]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:55 2008'' |
Revision as of 14:37, 21 February 2008
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CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION CHAPERONE SYCT
Overview
Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 angstroms resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT(C139S) is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT.
About this Structure
2BHO is a Single protein structure of sequence from Yersinia enterocolitica with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT., Locher M, Lehnert B, Krauss K, Heesemann J, Groll M, Wilharm G, J Biol Chem. 2005 Sep 2;280(35):31149-55. Epub 2005 Jul 6. PMID:16000312
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