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7Z0K

human PEX13 SH3 in complex with PEX5 W4 (WxxxF/Y) motif

Summary for 7Z0K
Entry DOI10.2210/pdb7z0k/pdb
DescriptorPeroxisomal membrane protein PEX13,Peroxisomal targeting signal 1 receptor (2 entities in total)
Functional Keywordsprotein transport, transport protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight23145.40
Authors
Gaussmann, S.,Napolitano, V.,sattler, M. (deposition date: 2022-02-23, release date: 2023-03-08, Last modification date: 2025-09-03)
Primary citationGaussmann, S.,Peschel, R.,Ott, J.,Zak, K.M.,Sastre, J.,Delhommel, F.,Popowicz, G.M.,Boekhoven, J.,Schliebs, W.,Erdmann, R.,Sattler, M.
Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.
Nat Commun, 15:3317-3317, 2024
Cited by
PubMed Abstract: Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. By combining biochemical methods and structural biology, we show that the C-terminal SH3 domain of PEX13 mediates intramolecular interactions with a proximal FxxxF motif. The SH3 domain also binds WxxxF peptide motifs in the import receptor PEX5, demonstrating evolutionary conservation of such interactions from yeast to human. Strikingly, intramolecular interaction of the PEX13 FxxxF motif regulates binding of PEX5 WxxxF/Y motifs to the PEX13 SH3 domain. Crystal structures reveal how FxxxF and WxxxF/Y motifs are recognized by a non-canonical surface on the SH3 domain. The PEX13 FxxxF motif also mediates binding to PEX14. Surprisingly, the potential PxxP binding surface of the SH3 domain does not recognize PEX14 PxxP motifs, distinct from its yeast ortholog. Our data show that the dynamic network of PEX13 interactions with PEX5 and PEX14, mediated by diaromatic peptide motifs, modulates peroxisomal matrix import.
PubMed: 38632234
DOI: 10.1038/s41467-024-47605-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

242842

数据于2025-10-08公开中

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