1g4u

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(New page: 200px<br /> <applet load="1g4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4u, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g4u.gif|left|200px]]<br />
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[[Image:1g4u.gif|left|200px]]<br /><applet load="1g4u" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1g4u" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1g4u, resolution 2.3&Aring;" />
caption="1g4u, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1'''<br />
'''CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1'''<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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1G4U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MG, GDP and AF3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4U OCA].
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1G4U is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=AF3:'>AF3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4U OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
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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: AF3]]
[[Category: AF3]]
[[Category: GDP]]
[[Category: GDP]]
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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 Mon Nov 12 17:00:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:06 2008''

Revision as of 10:46, 21 February 2008

Image:1g4u.gif

1g4u, resolution 2.3Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1

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

1G4U is a Protein complex structure of sequences from Homo sapiens and Salmonella typhimurium with , and as ligands. 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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