Summary for 5MY3
| Entry DOI | 10.2210/pdb5my3/pdb |
| Descriptor | RHO GTPase-activating protein RGD1 (2 entities in total) |
| Functional Keywords | rhogap, rgd1, polarized growth, cytokinesis, cell cycle |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Cellular location | Cytoplasm : P38339 |
| Total number of polymer chains | 1 |
| Total formula weight | 25723.57 |
| Authors | Martinez, D.M.,d'Estaintot, B.L.,Granier, T.,Hugues, M.,Odaert, B.,Gallois, B.,Doignon, F. (deposition date: 2017-01-25, release date: 2018-01-24, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 28760887DOI: 10.1042/BCJ20170331 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
Download full validation report
