2ocy

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(New page: 200px<br /><applet load="2ocy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ocy, resolution 3.3&Aring;" /> '''Complex of the guanin...)
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[[Image:2ocy.jpg|left|200px]]<br /><applet load="2ocy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ocy.jpg|left|200px]]<br /><applet load="2ocy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ocy, resolution 3.3&Aring;" />
caption="2ocy, resolution 3.3&Aring;" />
'''Complex of the guanine exchange factor Sec2p and the Rab GTPase Sec4p'''<br />
'''Complex of the guanine exchange factor Sec2p and the Rab GTPase Sec4p'''<br />
==Overview==
==Overview==
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Rab GTPases, the largest subgroup in the superfamily of Ras-like GTPases, play regulatory roles in multiple steps of intracellular vesicle, trafficking. They are activated by guanine nucleotide exchange factors, (GEFs), which catalyze the interconversion of the GDP-bound, or inactive, form of Rab to the GTP-bound, or active, form. Relatively little is known, of the mechanisms by which GEFs activate Rabs. Here, we present the, crystal structure of the GEF domain of Sec2p in complex with its Rab, partner Sec4p. The Sec2p GEF domain is a 220 Angstroms long coiled coil, striking in its simplicity and in the use of the coiled-coil motif for, catalysis. The structure suggests a mechanism whereby Sec2p induces, extensive structural rearrangements in the Sec4p switch regions and, phosphate-binding loop that are incompatible with nucleotide binding. We, show that Sec2p is specific for Sec4p and that specificity determinants, reside in the two switch regions of Sec4p.
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Rab GTPases, the largest subgroup in the superfamily of Ras-like GTPases, play regulatory roles in multiple steps of intracellular vesicle trafficking. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the interconversion of the GDP-bound, or inactive, form of Rab to the GTP-bound, or active, form. Relatively little is known of the mechanisms by which GEFs activate Rabs. Here, we present the crystal structure of the GEF domain of Sec2p in complex with its Rab partner Sec4p. The Sec2p GEF domain is a 220 Angstroms long coiled coil, striking in its simplicity and in the use of the coiled-coil motif for catalysis. The structure suggests a mechanism whereby Sec2p induces extensive structural rearrangements in the Sec4p switch regions and phosphate-binding loop that are incompatible with nucleotide binding. We show that Sec2p is specific for Sec4p and that specificity determinants reside in the two switch regions of Sec4p.
==About this Structure==
==About this Structure==
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2OCY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OCY OCA].
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2OCY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCY OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Dong, G.]]
[[Category: Dong, G.]]
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[[Category: Reinisch, K.M.]]
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[[Category: Reinisch, K M.]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
[[Category: gef]]
[[Category: gef]]
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[[Category: rab]]
[[Category: rab]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:07:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:05 2008''

Revision as of 16:17, 21 February 2008


2ocy, resolution 3.3Å

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Complex of the guanine exchange factor Sec2p and the Rab GTPase Sec4p

Overview

Rab GTPases, the largest subgroup in the superfamily of Ras-like GTPases, play regulatory roles in multiple steps of intracellular vesicle trafficking. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the interconversion of the GDP-bound, or inactive, form of Rab to the GTP-bound, or active, form. Relatively little is known of the mechanisms by which GEFs activate Rabs. Here, we present the crystal structure of the GEF domain of Sec2p in complex with its Rab partner Sec4p. The Sec2p GEF domain is a 220 Angstroms long coiled coil, striking in its simplicity and in the use of the coiled-coil motif for catalysis. The structure suggests a mechanism whereby Sec2p induces extensive structural rearrangements in the Sec4p switch regions and phosphate-binding loop that are incompatible with nucleotide binding. We show that Sec2p is specific for Sec4p and that specificity determinants reside in the two switch regions of Sec4p.

About this Structure

2OCY is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p., Dong G, Medkova M, Novick P, Reinisch KM, Mol Cell. 2007 Feb 9;25(3):455-62. PMID:17289591

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