2C5Z
Structure and CTD binding of the Set2 SRI domain
Summary for 2C5Z
| Entry DOI | 10.2210/pdb2c5z/pdb |
| Related | 1E0N |
| Descriptor | SET DOMAIN PROTEIN 2 (1 entity in total) |
| Functional Keywords | sri domain, rna polymerase ii, transcription, ctd, set2 histone methyltransferase |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Nucleus: P46995 |
| Total number of polymer chains | 1 |
| Total formula weight | 11982.03 |
| Authors | Vojnic, E.,Simon, B.,Strahl, B.D.,Sattler, M.,Cramer, P. (deposition date: 2005-11-03, release date: 2005-11-14, Last modification date: 2024-05-15) |
| Primary citation | Vojnic, E.,Simon, B.,Strahl, B.D.,Sattler, M.,Cramer, P. Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription. J. Biol. Chem., 281:13-15, 2006 Cited by PubMed Abstract: During mRNA elongation, the SRI domain of the histone H3 methyltransferase Set2 binds to the phosphorylated carboxyl-terminal domain (CTD) of RNA polymerase II. The solution structure of the yeast Set2 SRI domain reveals a novel CTD-binding fold consisting of a left-handed three-helix bundle. NMR titration shows that the SRI domain binds an Ser2/Ser5-phosphorylated CTD peptide comprising two heptapeptide repeats and three flanking NH2-terminal residues, whereas a single CTD repeat is insufficient for binding. Residues that show strong chemical shift perturbations upon CTD binding cluster in two regions. Both CTD tyrosine side chains contact the SRI domain. One of the tyrosines binds in the region with the strongest chemical shift perturbations, formed by the two NH2-terminal helices. Unexpectedly, the SRI domain fold resembles the structure of an RNA polymerase-interacting domain in bacterial sigma factors (domain sigma2 in sigma70). PubMed: 16286474DOI: 10.1074/jbc.C500423200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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