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Complex of Arl2 and PDE delta, Crystal Form 1

Overview

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.

About this Structure

1KSG is a Protein complex structure of sequences from Homo sapiens and Mus musculus with MG and GTP as ligands. Active as 3',5'-cyclic-nucleotide phosphodiesterase, with EC number 3.1.4.17 Full crystallographic information is available from OCA.

Reference

The complex of Arl2-GTP and PDE delta: from structure to function., Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC, EMBO J. 2002 May 1;21(9):2095-106. PMID:11980706

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