1g4w: Difference between revisions
New page: left|200px<br /><applet load="1g4w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4w, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1g4w.jpg|left|200px]]<br /><applet load="1g4w" size=" | [[Image:1g4w.jpg|left|200px]]<br /><applet load="1g4w" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1g4w, resolution 2.2Å" /> | caption="1g4w, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP'''<br /> | '''CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP'''<br /> | ||
==Overview== | ==Overview== | ||
Salmonella spp. utilize a specialized protein secretion system to deliver | Salmonella spp. utilize a specialized protein secretion system to deliver a battery of effector proteins into host cells. Several of these effectors stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote bacterial internalization. These potentially cytotoxic alterations are rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution crystal structure of an SptP-Rac1 transition state complex reveals an unusual GAP architecture that mimics host functional homologs. The phosphatase domain possesses a conserved active site but distinct surface properties. Binding to Rac1 induces a dramatic stabilization in SptP of a four-helix bundle that makes extensive contacts with the Switch I and Switch II regions of the GTPase. | ||
==About this Structure== | ==About this Structure== | ||
1G4W 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:// | 1G4W 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=1G4W OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Galan, J | [[Category: Galan, J E.]] | ||
[[Category: Stebbins, C | [[Category: Stebbins, C E.]] | ||
[[Category: 4-helix bundle]] | [[Category: 4-helix bundle]] | ||
[[Category: disorder]] | [[Category: disorder]] | ||
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[[Category: virulence factor]] | [[Category: virulence factor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:16 2008'' | ||
Revision as of 10:46, 21 February 2008
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CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP
Overview
Salmonella spp. utilize a specialized protein secretion system to deliver a battery of effector proteins into host cells. Several of these effectors stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote bacterial internalization. These potentially cytotoxic alterations are rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution crystal structure of an SptP-Rac1 transition state complex reveals an unusual GAP architecture that mimics host functional homologs. The phosphatase domain possesses a conserved active site but distinct surface properties. Binding to Rac1 induces a dramatic stabilization in SptP of a four-helix bundle that makes extensive contacts with the Switch I and Switch II regions of the GTPase.
About this Structure
1G4W is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1., Stebbins CE, Galan JE, Mol Cell. 2000 Dec;6(6):1449-60. PMID:11163217
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