7E29
Crystal Structure of Saccharomyces cerevisiae Ioc4 PWWP domain fused with MBP
Summary for 7E29
| Entry DOI | 10.2210/pdb7e29/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltose/maltodextrin-binding periplasmic protein,ISWI one complex protein 4, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | pwwp, transcription, gene regulation |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 1 |
| Total formula weight | 61687.84 |
| Authors | Li, J.,Smolle, M.,Liang, H.,Liu, Y. (deposition date: 2021-02-05, release date: 2022-02-09, Last modification date: 2023-11-29) |
| Primary citation | Li, J.,Bergmann, L.,Rafael de Almeida, A.,Webb, K.M.,Gogol, M.M.,Voigt, P.,Liu, Y.,Liang, H.,Smolle, M.M. H3K36 methylation and DNA-binding both promote Ioc4 recruitment and Isw1b remodeler function. Nucleic Acids Res., 50:2549-2565, 2022 Cited by PubMed Abstract: The Isw1b chromatin-remodeling complex is specifically recruited to gene bodies to help retain pre-existing histones during transcription by RNA polymerase II. Recruitment is dependent on H3K36 methylation and the Isw1b subunit Ioc4, which contains an N-terminal PWWP domain. Here, we present the crystal structure of the Ioc4-PWWP domain, including a detailed functional characterization of the domain on its own as well as in the context of full-length Ioc4 and the Isw1b remodeler. The Ioc4-PWWP domain preferentially binds H3K36me3-containing nucleosomes. Its ability to bind DNA is required for nucleosome binding. It is also furthered by the unique insertion motif present in Ioc4-PWWP. The ability to bind H3K36me3 and DNA promotes the interaction of full-length Ioc4 with nucleosomes in vitro and they are necessary for its recruitment to gene bodies in vivo. Furthermore, a fully functional Ioc4-PWWP domain promotes efficient remodeling by Isw1b and the maintenance of ordered chromatin in vivo, thereby preventing the production of non-coding RNAs. PubMed: 35188579DOI: 10.1093/nar/gkac077 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.303 Å) |
Structure validation
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