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1txu

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==Overview==
==Overview==
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The Rab5 GTPase, an essential regulator of endocytosis and endosome, biogenesis, is activated by guanine-nucleotide exchange factors (GEFs), that contain a Vps9 domain. Here, we show that the catalytic core of the, Rab GEF Rabex-5 has a tandem architecture consisting of a Vps9 domain, stabilized by an indispensable helical bundle. A family-wide analysis of, Rab specificity demonstrates high selectivity for Rab5 subfamily GTPases., Conserved exchange determinants map to a common surface of the Vps9, domain, which recognizes invariant aromatic residues in the switch regions, of Rab GTPases and selects for the Rab5 subfamily by requiring a small, nonacidic residue preceding a critical phenylalanine in the switch I, region. These and other observations reveal unexpected similarity with the, Arf exchange site in the Sec7 domain.
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The Rab5 GTPase, an essential regulator of endocytosis and endosome biogenesis, is activated by guanine-nucleotide exchange factors (GEFs) that contain a Vps9 domain. Here, we show that the catalytic core of the Rab GEF Rabex-5 has a tandem architecture consisting of a Vps9 domain stabilized by an indispensable helical bundle. A family-wide analysis of Rab specificity demonstrates high selectivity for Rab5 subfamily GTPases. Conserved exchange determinants map to a common surface of the Vps9 domain, which recognizes invariant aromatic residues in the switch regions of Rab GTPases and selects for the Rab5 subfamily by requiring a small nonacidic residue preceding a critical phenylalanine in the switch I region. These and other observations reveal unexpected similarity with the Arf exchange site in the Sec7 domain.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Delprato, A.]]
[[Category: Delprato, A.]]
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[[Category: Lambright, D.G.]]
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[[Category: Lambright, D G.]]
[[Category: Merithew, E.]]
[[Category: Merithew, E.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: vps9 domain]]
[[Category: vps9 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:58:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:30 2008''

Revision as of 13:18, 21 February 2008


1txu, resolution 2.35Å

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Crystal Structure of the Vps9 Domain of Rabex-5

Overview

The Rab5 GTPase, an essential regulator of endocytosis and endosome biogenesis, is activated by guanine-nucleotide exchange factors (GEFs) that contain a Vps9 domain. Here, we show that the catalytic core of the Rab GEF Rabex-5 has a tandem architecture consisting of a Vps9 domain stabilized by an indispensable helical bundle. A family-wide analysis of Rab specificity demonstrates high selectivity for Rab5 subfamily GTPases. Conserved exchange determinants map to a common surface of the Vps9 domain, which recognizes invariant aromatic residues in the switch regions of Rab GTPases and selects for the Rab5 subfamily by requiring a small nonacidic residue preceding a critical phenylalanine in the switch I region. These and other observations reveal unexpected similarity with the Arf exchange site in the Sec7 domain.

About this Structure

1TXU is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5., Delprato A, Merithew E, Lambright DG, Cell. 2004 Sep 3;118(5):607-17. PMID:15339665

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