6G04
NMR Solution Structure of Yeast TSR2(1-152) in Complex with S26A(100-119)
Summary for 6G04
| Entry DOI | 10.2210/pdb6g04/pdb |
| Related | 6G03 |
| NMR Information | BMRB: 34248 |
| Descriptor | Pre-rRNA-processing protein TSR2, 40S ribosomal protein S26-A (2 entities in total) |
| Functional Keywords | ribosome maturation, transport of ribosomal protein s26, nuclear unloading factor, escortin, nucleus, alpha-helical protein, eukaryotic specific segments, transport protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 20841.37 |
| Authors | Michel, E.,Schuetz, S.,Damberger, F.F.,Allain, F.H.-T.,Panse, V.G. (deposition date: 2018-03-16, release date: 2018-09-19, Last modification date: 2024-05-15) |
| Primary citation | Schutz, S.,Michel, E.,Damberger, F.F.,Oplova, M.,Pena, C.,Leitner, A.,Aebersold, R.,Allain, F.H.,Panse, V.G. Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2. Nat Commun, 9:3669-3669, 2018 Cited by PubMed Abstract: Disordered extensions at the termini and short internal insertions distinguish eukaryotic ribosomal proteins (r-proteins) from their anucleated archaeal counterparts. Here, we report an NMR structure of such a eukaryotic-specific segment (ESS) in the r-protein eS26 in complex with the escortin Tsr2. The structure reveals how ESS attracts Tsr2 specifically to importin:eS26 complexes entering the nucleus in order to trigger non-canonical RanGTP-independent disassembly. Tsr2 then sequesters the released eS26 and prevents rebinding to the importin, providing an alternative allosteric mechanism to terminate the process of nuclear import. Notably, a Diamond-Blackfan anemia-associated Tsr2 mutant protein is impaired in binding to ESS, unveiling a critical role for this interaction in human hematopoiesis. We propose that eS26-ESS and Tsr2 are components of a nuclear sorting system that co-evolved with the emergence of the nucleocytoplasmic barrier and transport carriers. PubMed: 30201955DOI: 10.1038/s41467-018-06160-x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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