3Q72

Crystal Structure of Rad G-domain-GTP Analog Complex

Summary for 3Q72

• Entry DOI: 10.2210/pdb3q72/pdb
• Related: 2DPX 3Q7P 3Q7Q
• Descriptor: GTP-binding protein RAD, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: g-domain, g-protein, cav2 beta, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane (By similarity): P55042
• Total number of polymer chains: 2
• Total formula weight: 37636.59

Authors

Sasson, Y.,Navon-Perry, L.,Hirsch, J.A. (deposition date: 2011-01-04, release date: 2011-09-21, Last modification date: 2024-02-21)

Primary citation

Sasson, Y.,Navon-Perry, L.,Huppert, D.,Hirsch, J.A.
RGK Family G-Domain:GTP Analog Complex Structures and Nucleotide-Binding Properties.
J.Mol.Biol., 413:372-389, 2011

PubMed Abstract: The RGK family of small G-proteins, including Rad, Gem, Rem1, and Rem2, is inducibly expressed in various mammalian tissues and interacts with voltage-dependent calcium channels and Rho kinase. Many questions remain regarding their physiological roles and molecular mechanism. Previous crystallographic studies reported RGK G-domain:guanosine di-phosphate structures. To test whether RGK proteins undergo a nucleotide-induced conformational change, we determined the crystallographic structures of Rad:GppNHp and Rem2:GppNHp to 1.7 and 1.8 Å resolutions, respectively. Also, we characterized the nucleotide-binding properties and conformations for Gem, Rad, and several structure-based mutants using fluorescence spectroscopy. The results suggest that RGK G-proteins may not behave as Ras-like canonical nucleotide-induced molecular switches. Further, the RGK proteins have differing structures and nucleotide-binding properties, which may have implications for their varied action on effectors.

PubMed: 21903096
DOI: 10.1016/j.jmb.2011.08.017

Experimental method

X-RAY DIFFRACTION (1.655 Å)