5MY3

Crystal structure of the RhoGAP domain of Rgd1p at 2.19 Angstroms resolution

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5MY3 の概要

• エントリーDOI: 10.2210/pdb5my3/pdb
• 分子名称: RHO GTPase-activating protein RGD1 (2 entities in total)
• 機能のキーワード: rhogap, rgd1, polarized growth, cytokinesis, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• 細胞内の位置: Cytoplasm : P38339
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25723.57

構造登録者

Martinez, D.M.,d'Estaintot, B.L.,Granier, T.,Hugues, M.,Odaert, B.,Gallois, B.,Doignon, F. (登録日: 2017-01-25, 公開日: 2018-01-24, 最終更新日: 2024-01-17)

主引用文献

Martinez, D.,Langlois d'Estaintot, B.,Granier, T.,Tolchard, J.,Courreges, C.,Prouzet-Mauleon, V.,Hugues, M.,Gallois, B.,Doignon, F.,Odaert, B.
Structural evidence of a phosphoinositide-binding site in the Rgd1-RhoGAP domain.
Biochem. J., 474:3307-3319, 2017

PubMed Abstract: Phosphoinositide lipids recruit proteins to the plasma membrane involved in the regulation of cytoskeleton organization and in signalling pathways that control cell polarity and growth. Among those, Rgd1p is a yeast GTPase-activating protein (GAP) specific for Rho3p and Rho4p GTPases, which control actin polymerization and stress signalling pathways. Phosphoinositides not only bind Rgd1p, but also stimulate its GAP activity on the membrane-anchored form of Rho4p. Both F-BAR (F-BAR FCH, and BAR) and RhoGAP domains of Rgd1p are involved in lipid interactions. In the Rgd1p-F-BAR domain, a phosphoinositide-binding site has been recently characterized. We report here the X-ray structure of the Rgd1p-RhoGAP domain, identify by NMR spectroscopy and confirm by docking simulations, a new but cryptic phosphoinositide-binding site, comprising contiguous A1, A1' and B helices. The addition of helix A1', unusual among RhoGAP domains, seems to be crucial for lipid interactions. Such a site was totally unexpected inside a RhoGAP domain, as it was not predicted from either the protein sequence or its three-dimensional structure. Phosphoinositide-binding sites in RhoGAP domains have been reported to correspond to polybasic regions, which are located at the unstructured flexible termini of proteins. Solid-state NMR spectroscopy experiments confirm the membrane interaction of the Rgd1p-RhoGAP domain upon the addition of PtdIns(4,5)P and indicate a slight membrane destabilization in the presence of the two partners.

PubMed: 28760887
DOI: 10.1042/BCJ20170331

実験手法

X-RAY DIFFRACTION (2.19 Å)