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7Z0I

human PEX13 SH3 domain

Summary for 7Z0I
Entry DOI10.2210/pdb7z0i/pdb
DescriptorPeroxisomal membrane protein PEX13, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsprotein transport
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight9589.08
Authors
Gaussmann, S.,Zak, K.,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 (1.8 Å)
Structure validation

243911

数据于2025-10-29公开中

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