2MPJ
NMR structure of Xenopus RecQ4 zinc knuckle
Summary for 2MPJ
| Entry DOI | 10.2210/pdb2mpj/pdb |
| NMR Information | BMRB: 19986 |
| Descriptor | RECQL4-helicase-like protein, ZINC ION (2 entities in total) |
| Functional Keywords | zinc knuckle, recq4, helicase, dna/rna binding, protein, nucleotide binding protein |
| Biological source | Xenopus laevis (clawed frog,common platanna,platanna) |
| Total number of polymer chains | 1 |
| Total formula weight | 2679.32 |
| Authors | Zucchelli, C.,Marino, F.,Mojumdar, A.,Onesti, S.,Musco, G. (deposition date: 2014-05-23, release date: 2015-08-05, Last modification date: 2024-05-15) |
| Primary citation | Marino, F.,Mojumdar, A.,Zucchelli, C.,Bhardwaj, A.,Buratti, E.,Vindigni, A.,Musco, G.,Onesti, S. Structural and biochemical characterization of an RNA/DNA binding motif in the N-terminal domain of RecQ4 helicases Sci Rep, 6:21501-21501, 2016 Cited by PubMed Abstract: The RecQ4 helicase belongs to the ubiquitous RecQ family but its exact role in the cell is not completely understood. In addition to the helicase domain, RecQ4 has a unique N-terminal part that is essential for viability and is constituted by a region homologous to the yeast Sld2 replication initiation factor, followed by a cysteine-rich region, predicted to fold as a Zn knuckle. We carried out a structural and biochemical analysis of both the human and Xenopus laevis RecQ4 cysteine-rich regions, and showed by NMR spectroscopy that the Xenopus fragment indeed assumes the canonical Zn knuckle fold, whereas the human sequence remains unstructured, consistent with the mutation of one of the Zn ligands. Both the human and Xenopus Zn knuckles bind to a variety of nucleic acid substrates, with a mild preference for RNA. We also investigated the effect of a segment located upstream the Zn knuckle that is highly conserved and rich in positively charged and aromatic residues, partially overlapping with the C-terminus of the Sld2-like domain. In both the human and Xenopus proteins, the presence of this region strongly enhances binding to nucleic acids. These results reveal novel possible roles of RecQ4 in DNA replication and genome stability. PubMed: 26888063DOI: 10.1038/srep21501 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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