7SXI
Solution Structure of Sds3 Capped Tudor Domain
Summary for 7SXI
| Entry DOI | 10.2210/pdb7sxi/pdb |
| NMR Information | BMRB: 30969 |
| Descriptor | Sin3 histone deacetylase corepressor complex component SDS3 (1 entity in total) |
| Functional Keywords | transcriptional corepressor, tudor domain, nucleic acid binding, g-quadruplex binding, gene regulation |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 9390.71 |
| Authors | Marcum, R.D.,Radhakrishnan, I. (deposition date: 2021-11-23, release date: 2022-01-19, Last modification date: 2024-05-15) |
| Primary citation | Marcum, R.D.,Hsieh, J.,Giljen, M.,Justice, E.,Daffern, N.,Zhang, Y.,Radhakrishnan, I. A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes. J.Biol.Chem., 298:101558-101558, 2022 Cited by PubMed Abstract: Chromatin-modifying complexes containing histone deacetylase (HDAC) activities play critical roles in the regulation of gene transcription in eukaryotes. These complexes are thought to lack intrinsic DNA-binding activity, but according to a well-established paradigm, they are recruited via protein-protein interactions by gene-specific transcription factors and posttranslational histone modifications to their sites of action on the genome. The mammalian Sin3L/Rpd3L complex, comprising more than a dozen different polypeptides, is an ancient HDAC complex found in diverse eukaryotes. The subunits of this complex harbor conserved domains and motifs of unknown structure and function. Here, we show that Sds3, a constitutively-associated subunit critical for the proper functioning of the Sin3L/Rpd3L complex, harbors a type of Tudor domain that we designate the capped Tudor domain. Unlike canonical Tudor domains that bind modified histones, the Sds3 capped Tudor domain binds to nucleic acids that can form higher-order structures such as G-quadruplexes and shares similarities with the knotted Tudor domain of the Esa1 histone acetyltransferase that was previously shown to bind single-stranded RNA. Our findings expand the range of macromolecules capable of recruiting the Sin3L/Rpd3L complex and draw attention to potentially new biological roles for this HDAC complex. PubMed: 34979096DOI: 10.1016/j.jbc.2021.101558 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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