1q5z
From Proteopedia
(New page: 200px<br /><applet load="1q5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q5z, resolution 1.8Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1q5z.jpg|left|200px]]<br /><applet load="1q5z" size=" | + | [[Image:1q5z.jpg|left|200px]]<br /><applet load="1q5z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q5z, resolution 1.8Å" /> | caption="1q5z, resolution 1.8Å" /> | ||
'''Crystal Structure of the C-terminal Actin Binding Domain of Salmonella Invasion Protein A (SipA)'''<br /> | '''Crystal Structure of the C-terminal Actin Binding Domain of Salmonella Invasion Protein A (SipA)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Like many bacterial pathogens, Salmonella spp. use a type III secretion | + | Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http:// | + | 1Q5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Egelman, E | + | [[Category: Egelman, E H.]] |
| - | [[Category: Galkin, V | + | [[Category: Galkin, V E.]] |
[[Category: Lilic, M.]] | [[Category: Lilic, M.]] | ||
[[Category: Orlova, A.]] | [[Category: Orlova, A.]] | ||
| - | [[Category: Stebbins, C | + | [[Category: Stebbins, C E.]] |
| - | [[Category: VanLoock, M | + | [[Category: VanLoock, M S.]] |
[[Category: cell invasion]] | [[Category: cell invasion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:12 2008'' |
Revision as of 12:36, 21 February 2008
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Crystal Structure of the C-terminal Actin Binding Domain of Salmonella Invasion Protein A (SipA)
Overview
Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.
About this Structure
1Q5Z is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms., Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE, Science. 2003 Sep 26;301(5641):1918-21. PMID:14512630
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