7PRD
Solution structure of the chimeric Nrd1-Nab3 heterodimerization domains
Summary for 7PRD
| Entry DOI | 10.2210/pdb7prd/pdb |
| NMR Information | BMRB: 34668 |
| Descriptor | Protein NRD1,HLJ1_G0022400.mRNA.1.CDS.1 (1 entity in total) |
| Functional Keywords | transcription termination, nns pathway, nab3, nrd1, heterodimerization, chimera, yeast, transcription |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 1 |
| Total formula weight | 13943.86 |
| Authors | Chaves-Arquero, B.,Martinez-Lumbreras, S.,Perez-Canadillas, J.M. (deposition date: 2021-09-21, release date: 2022-01-12, Last modification date: 2024-06-19) |
| Primary citation | Chaves-Arquero, B.,Martinez-Lumbreras, S.,Camero, S.,Santiveri, C.M.,Mirassou, Y.,Campos-Olivas, R.,Jimenez, M.A.,Calvo, O.,Perez-Canadillas, J.M. Structural basis of Nrd1-Nab3 heterodimerization. Life Sci Alliance, 5:-, 2022 Cited by PubMed Abstract: Heterodimerization of RNA binding proteins Nrd1 and Nab3 is essential to communicate the RNA recognition in the nascent transcript with the Nrd1 recognition of the Ser-phosphorylated Rbp1 C-terminal domain in RNA polymerase II. The structure of a Nrd1-Nab3 chimera reveals the basis of heterodimerization, filling a missing gap in knowledge of this system. The free form of the Nrd1 interaction domain of Nab3 (NRID) forms a multi-state three-helix bundle that is clamped in a single conformation upon complex formation with the Nab3 interaction domain of Nrd1 (NAID). The latter domain forms two long helices that wrap around NRID, resulting in an extensive protein-protein interface that would explain the highly favorable free energy of heterodimerization. Mutagenesis of some conserved hydrophobic residues involved in the heterodimerization leads to temperature-sensitive phenotypes, revealing the importance of this interaction in yeast cell fitness. The Nrd1-Nab3 structure resembles the previously reported Rna14/Rna15 heterodimer structure, which is part of the poly(A)-dependent termination pathway, suggesting that both machineries use similar structural solutions despite they share little sequence homology and are potentially evolutionary divergent. PubMed: 35022249DOI: 10.26508/lsa.202101252 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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