1NM7
Solution structure of the ScPex13p SH3 domain
Summary for 1NM7
| Entry DOI | 10.2210/pdb1nm7/pdb |
| Related | 1N5Z |
| Descriptor | Peroxisomal Membrane Protein PAS20 (1 entity in total) |
| Functional Keywords | yeast, membrane protein, pex5p, pex14p, pex13p, import machine, sh3 domain, protein transport |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Peroxisome membrane; Single-pass membrane protein: P80667 |
| Total number of polymer chains | 1 |
| Total formula weight | 8086.21 |
| Authors | Pires, J.R.,Hong, X.,Brockmann, C.,Volkmer-Engert, R.,Schneider-Mergener, J.,Oschkinat, H.,Erdmann, R. (deposition date: 2003-01-09, release date: 2003-03-04, Last modification date: 2024-05-29) |
| Primary citation | Pires, J.R.,Hong, X.,Brockmann, C.,Volkmer-Engert, R.,Schneider-Mergener, J.,Oschkinat, H.,Erdmann, R. The ScPex13p SH3 Domain Exposes Two Distinct Binding Sites for Pex5p and Pex14p J.Mol.Biol., 326:1427-1435, 2003 Cited by PubMed Abstract: Pex13p is an essential component of the peroxisomal protein import machinery and interacts via its C-terminal SH3 domain with the type II SH3-ligand Pex14p and the non-PXXP protein Pex5p. We report the solution structure of the SH3 domain of Pex13p from Saccharomyces cerevisiae and the identification of a novel-binding pocket, which binds a non-PXXP-peptide representing the binding site of Pex5p. Chemical shift assays revealed the binding sites for Pex5p and Pex14p ligand peptides to be distinct and spatially separated. Competition assays demonstrated that the two ligand peptides can bind simultaneously to the SH3 domain. PubMed: 12595255DOI: 10.1016/S0022-2836(03)00039-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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