1g4w

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(New page: 200px<br /><applet load="1g4w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4w, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1g4w.jpg|left|200px]]<br /><applet load="1g4w" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1g4w, resolution 2.2&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4W OCA].
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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]]
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[[Category: Galan, J.E.]]
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[[Category: Galan, J E.]]
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[[Category: Stebbins, C.E.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:42:31 2007''
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''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


1g4w, resolution 2.2Å

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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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