3BH7

Crystal structure of the RP2-Arl3 complex bound to GDP-AlF4

Summary for 3BH7

• Entry DOI: 10.2210/pdb3bh7/pdb
• Related: 2BX6 3BH6
• Descriptor: ADP-ribosylation factor-like protein 3, Protein XRP2, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: protein-protein complex, gtpase activating protein and gtpase, retinitis pigmentosa, gtp-binding, lipoprotein, myristate, nucleotide-binding, disease mutation, membrane, palmitate, phosphoprotein, sensory transduction, vision, metal binding protein, signaling protein
• Biological source: Mus musculus (house mouse); More
• Cellular location: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side: Q9WUL7; Cell membrane; Lipid-anchor; Cytoplasmic side: O75695
• Total number of polymer chains: 2
• Total formula weight: 58782.38

Authors

Veltel, S.,Gasper, R.,Wittinghofer, A. (deposition date: 2007-11-28, release date: 2008-03-25, Last modification date: 2023-11-01)

Primary citation

Veltel, S.,Gasper, R.,Eisenacher, E.,Wittinghofer, A.
The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3
Nat.Struct.Mol.Biol., 15:373-380, 2008

PubMed Abstract: The retinitis pigmentosa 2 (RP2) gene is responsible for a particular variant of X chromosome-linked eye disease. Previously, RP2 was shown to bind the GTP form of the small G protein Arf-like 3 (Arl3), thus qualifying as an effector. Here we present the Arl3-GppNHp-RP2 complex structure, which shows features resembling complexes with GTPase-activating proteins (GAPs). Biochemical analysis showing a 90,000-fold stimulation of the GTPase reaction together with the structure of an Arl3-GDP-AlF4--RP2 transition state complex showed that RP2 is an efficient GAP for Arl3, with structural features similar to other GAPs. Furthermore, the effect of mutations in patients with retinitis pigmentosa correlated with their effect on catalysis, in particular the mutation of the arginine finger of RP2. The cognate G protein-GAP pair is conserved in yeast as Cin4-Cin2, and the ability of RP2 to act as a GAP can be correlated with its ability to complement a CIN2-deletion phenotype.

PubMed: 18376416
DOI: 10.1038/nsmb.1396

Experimental method

X-RAY DIFFRACTION (1.9 Å)