1dcq
From Proteopedia
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CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.
Overview
ADP ribosylation factors (ARFs), which are members of the Ras superfamily, of GTP-binding proteins, are critical components of vesicular trafficking, pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins, (GAPs), which assist ARFs in hydrolyzing GTP to GDP. PAPbeta, a protein, that binds to and is phosphorylated by the non-receptor tyrosine kinase, PYK2, contains several modular signaling domains including a pleckstrin, homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain., Sequences of ARF-GAP domains show no recognizable similarity to those of, other GAPs, and contain a characteristic, Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. The crystal structure of the, PAPbeta ARF-GAP domain and the C-terminal ankyrin repeats has been, determined at 2.1 A resolution. The ARF-GAP domain comprises a central, three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion, coordinated by the four cysteines of the cysteine-rich motif. Four ankyrin, repeats are also present, the first two of which form an extensive, interface with the ARF-GAP domain. An invariant arginine and several, nearby hydrophobic residues are solvent exposed and are predicted to be, the site of interaction with ARFs. Site-directed mutagenesis of these, residues confirms their importance in ARF-GAP activity.
About this Structure
1DCQ is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta., Mandiyan V, Andreev J, Schlessinger J, Hubbard SR, EMBO J. 1999 Dec 15;18(24):6890-8. PMID:10601011
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