7OIY
Crystal structure of the ZUFSP family member Mug105
Summary for 7OIY
| Entry DOI | 10.2210/pdb7oiy/pdb |
| Descriptor | Ubiquitin carboxyl-terminal hydrolase mug105, SODIUM ION (3 entities in total) |
| Functional Keywords | zufsp, deubiquitinase, schizosaccharomyces pombe, fission yeast, cysteine peptidase, k48, hydrolase |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 56273.82 |
| Authors | Pichlo, C.,Hermanns, T.,Hofmann, K.,Baumann, U. (deposition date: 2021-05-12, release date: 2022-02-02, Last modification date: 2024-01-31) |
| Primary citation | Hermanns, T.,Pichlo, C.,Baumann, U.,Hofmann, K. A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family. Nat Commun, 13:401-401, 2022 Cited by PubMed Abstract: Eukaryotic deubiquitinases are important regulators of ubiquitin signaling and can be subdivided into several structurally distinct classes. The ZUFSP family, with ZUP1 as its sole human member, has a modular architecture with a core catalytic domain highly active against the ubiquitin-derived peptide RLRGG, but not against ubiquitin itself. Ubiquitin recognition is conferred by additional non-catalytic domains, making full-length ZUP1 active against long K63-linked chains. However, non-mammalian ZUFSP family members contain different ubiquitin-binding domains in their N-terminal regions, despite their high conservation within the catalytic domain. Here, by working with representative ZUFSP family members from insects, fungi and plants, we show that different N-terminal domains are associated with different linkage preferences. Biochemical and structural studies suggest that the acquisition of two family-specific proximal domains have changed the default K48 preference of the ZUFSP family to the K63 preference observed in ZUP1 and its insect homolog. Additional N-terminal zinc finger domains promote chain cleavage without changing linkage-specificity. PubMed: 35058438DOI: 10.1038/s41467-022-28049-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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