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5YT6

Crystal structure of TAX1BP1 UBZ2 in complex with mono-ubiquitin

Summary for 5YT6
Entry DOI10.2210/pdb5yt6/pdb
DescriptorUbiquitin, Tax1-binding protein 1, ZINC ION, ... (7 entities in total)
Functional Keywordstax1bp1, ubiquitin, complex, autophagy receptor, protein binding
Biological sourceHomo sapiens (Human)
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Total number of polymer chains8
Total formula weight52522.55
Authors
Pan, L.,Hu, S. (deposition date: 2017-11-17, release date: 2018-07-11, Last modification date: 2023-11-22)
Primary citationHu, S.,Wang, Y.,Gong, Y.,Liu, J.,Li, Y.,Pan, L.
Mechanistic Insights into Recognitions of Ubiquitin and Myosin VI by Autophagy Receptor TAX1BP1.
J. Mol. Biol., 430:3283-3296, 2018
Cited by
PubMed Abstract: TAX1BP1, a ubiquitin-binding adaptor, plays critical roles in the innate immunity and selective autophagy. During autophagy, TAX1BP1 may not only function as an autophagy receptor to recruit ubiquitylated substrates for autophagic degradation, but also serve as a Myosin VI cargo adaptor protein for mediating the maturation of autophagosome. However, the mechanistic basis underlying the specific interactions of TAX1BP1 with ubiquitin and Myosin VI remains elusive. Here, using biochemical, NMR and structural analyses, we elucidate the detailed binding mechanism and uncover the key determinants for the interaction between TAX1BP1 and ubiquitin. In addition, we reveal that both tandem zinc-fingers of TAX1BP1 and the conformational rigidity between them are required for the Myosin VI binding of TAX1BP1, and ubiquitin and Myosin VI are mutually exclusive in binding to TAX1BP1. Collectively, our findings provide mechanistic insights into the dual functions of TAX1BP1 in selective autophagy.
PubMed: 29940186
DOI: 10.1016/j.jmb.2018.06.030
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.501 Å)
Structure validation

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