1JO8

Structural analysis of the yeast actin binding protein Abp1 SH3 domain

Summary for 1JO8

• Entry DOI: 10.2210/pdb1jo8/pdb
• Descriptor: ACTIN BINDING PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: sh3 domain actin-binding-protein, structural protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm, cytoskeleton, actin patch: P15891
• Total number of polymer chains: 1
• Total formula weight: 6855.21

Authors

Fazi, B.,Cope, M.J.,Douangamath, A.,Ferracuti, S.,Schirwitz, K.,Zucconi, A.,Drubin, D.G.,Wilmanns, M.,Cesareni, G.,Castagnoli, L. (deposition date: 2001-07-27, release date: 2002-03-01, Last modification date: 2023-08-16)

Primary citation

Fazi, B.,Cope, M.J.,Douangamath, A.,Ferracuti, S.,Schirwitz, K.,Zucconi, A.,Drubin, D.G.,Wilmanns, M.,Cesareni, G.,Castagnoli, L.
Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis.
J.Biol.Chem., 277:5290-5298, 2002

PubMed Abstract: Abp1p is an actin-binding protein that plays a central role in the organization of Saccharomyces cerevisiae actin cytoskeleton. By a combination of two-hybrid and phage-display approaches, we have identified six new ligands of the Abp1-SH3 domain. None of these SH3-mediated novel interactions was detected in recent all genome high throughput protein interaction projects. Here we show that the SH3-mediated association of Abp1p with the Ser/Thr kinases Prk1p and Ark1p is essential for their localization to actin cortical patches. The Abp1-SH3 domain has a rather unusual binding specificity, because its target peptides contain the tetrapentapeptide +XXXPXXPX+PXXL with positive charges flanking the polyproline core on both sides. Here we present the structure of the Abp1-SH3 domain solved at 1.3-A resolution. The peptide-binding pockets in the SH3 domain are flanked by two acidic residues that are uncommon at those positions in the SH3 domain family. We have shown by site-directed mutagenesis that one of these negatively charged side chains may be the key determinant for the preference for non-classical ligands.

PubMed: 11668184
DOI: 10.1074/jbc.M109848200

Experimental method

X-RAY DIFFRACTION (1.3 Å)