1N5Z

Complex structure of Pex13p SH3 domain with a peptide of Pex14p

Summary for 1N5Z

• Entry DOI: 10.2210/pdb1n5z/pdb
• Descriptor: Peroxisomal membrane protein PAS20, 14-mer peptide from Peroxisomal membrane protein PEX14 (3 entities in total)
• Functional Keywords: sh3 domain, pxxp motif, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Peroxisome membrane; Single-pass membrane protein: P80667; Peroxisome membrane; Peripheral membrane protein; Cytoplasmic side: P53112
• Total number of polymer chains: 4
• Total formula weight: 24956.40

Authors

Douangamath, A.,Filipp, F.V.,Klein, A.T.J.,Barnett, P.,Zou, P.,Voorn-Brouwer, T.,Vega, M.C.,Mayans, O.M.,Sattler, M.,Distel, B.,Wilmanns, M. (deposition date: 2002-11-08, release date: 2002-12-11, Last modification date: 2024-03-13)

Primary citation

Douangamath, A.,Filipp, F.V.,Klein, A.T.J.,Barnett, P.,Zou, P.,Voorn-Brouwer, T.,Vega, M.C.,Mayans, O.M.,Sattler, M.,Distel, B.,Wilmanns, M.
Topography for Independent Binding of alpha-Helical and PPII-Helical Ligands to a Peroxisomal SH3 Domain
MOL.CELL, 10:1007-1017, 2002

PubMed Abstract: While the function of most small signaling domains is confined to binary ligand interactions, the peroxisomal Pex13p SH3 domain has the unique capacity of binding to two different ligands, Pex5p and Pex14p. We have used this domain as a model to decipher its structurally independent ligand binding sites. By the combined use of X-ray crystallography, NMR spectroscopy, and circular dichroism, we show that the two ligands bind in unrelated conformations to patches located at opposite surfaces of this SH3 domain. Mutations in the Pex13p SH3 domain that abolish interactions within the Pex13p-Pex5p interface specifically impair PTS1-dependent protein import into yeast peroxisomes.

PubMed: 12453410
DOI: 10.1016/S1097-2765(02)00749-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)