1KSH
Complex of Arl2 and PDE delta, Crystal Form 2 (native)
Summary for 1KSH
Entry DOI | 10.2210/pdb1ksh/pdb |
Related | 1KSG 1KSJ 1doa 1fzq |
Descriptor | arf-like protein 2, RETINAL ROD RHODOPSIN-SENSITIVE CGMP 3',5'-CYCLIC PHOSPHODIESTERASE DELTA-SUBUNIT, MAGNESIUM ION, ... (6 entities in total) |
Functional Keywords | small gtpase, small gtp-binding protein, arf family, effector molecule, immunoglobuline-like fold, gdi, signaling protein-hydrolase complex, signaling protein/hydrolase |
Biological source | Mus musculus (house mouse) More |
Cellular location | Mitochondrion intermembrane space: Q9D0J4 |
Total number of polymer chains | 2 |
Total formula weight | 39333.89 |
Authors | Hanzal-Bayer, M.,Renault, L.,Roversi, P.,Wittinghofer, A.,Hillig, R.C. (deposition date: 2002-01-13, release date: 2002-05-08, Last modification date: 2024-11-06) |
Primary citation | Hanzal-Bayer, M.,Renault, L.,Roversi, P.,Wittinghofer, A.,Hillig, R.C. The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J., 21:2095-2106, 2002 Cited by PubMed Abstract: Arf-like (Arl) proteins are close relatives of the Arf regulators of vesicular transport, but their function is unknown. Here, we present the crystal structure of full-length Arl2-GTP in complex with its effector PDE delta solved in two crystal forms (Protein Data Bank codes 1KSG, 1KSH and 1KSJ). Arl2 shows a dramatic conformational change from the GDP-bound form, which suggests that it is reversibly membrane associated. PDE delta is structurally closely related to RhoGDI and contains a deep empty hydrophobic pocket. Further experiments show that H-Ras, Rheb, Rho6 and G alpha(i1) interact with PDE delta and that, at least for H-Ras, the intact C-terminus is required. We suggest PDE delta to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDE delta-mediated transport. PubMed: 11980706DOI: 10.1093/emboj/21.9.2095 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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