4RJ9

Structure of a plant specific C2 domain protein, OsGAP1 from rice

Summary for 4RJ9

• Entry DOI: 10.2210/pdb4rj9/pdb
• Descriptor: C2 domain-containing protein-like, POTASSIUM ION (3 entities in total)
• Functional Keywords: beta_sandwich, lipid selectivity, calcium-dependent, phospholipid binding, membrane targeting, cytosol, ligase
• Biological source: Oryza sativa Japonica Group (Japonica rice)
• Cellular location: Cell membrane : Q6YWF1
• Total number of polymer chains: 1
• Total formula weight: 18651.81

Authors

Miao, R.,Fong, Y.H.,Wong, K.B.,Lam, H.M. (deposition date: 2014-10-08, release date: 2015-08-26, Last modification date: 2023-09-20)

Primary citation

Yung, Y.L.,Cheung, M.Y.,Miao, R.,Fong, Y.H.,Li, K.P.,Yu, M.H.,Chye, M.L.,Wong, K.B.,Lam, H.M.
Site-directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 for the Physiological Functions of the Rice GTPase-activating Protein 1 (OsGAP1).
J.Biol.Chem., 290:23984-23996, 2015

PubMed Abstract: The C2 domain is one of the most diverse phospholipid-binding domains mediating cellular signaling. One group of C2-domain proteins are plant-specific and are characterized by their small sizes and simple structures. We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1. Here we solved the crystal structure of OsGAP1 to a resolution of 1.63 Å. Using site-directed mutagenesis, we successfully differentiated between the clusters of surface residues that are required for binding to phospholipids versus OsYchF1, which, in turn, is critical for its role in stimulating defense responses. On the other hand, the ability to alleviate salt stress by OsGAP1 is dependent only on its ability to bind OsYchF1 and is independent of its phospholipid-binding activity.

PubMed: 26286751
DOI: 10.1074/jbc.M115.655639

Experimental method

X-RAY DIFFRACTION (1.63 Å)