2RIM
Crystal structure of Rtt109
Summary for 2RIM
| Entry DOI | 10.2210/pdb2rim/pdb |
| Descriptor | Regulator of Ty1 transposition protein 109 (2 entities in total) |
| Functional Keywords | rtt109 structure, dna damage, dna repair, nucleus, transcription, transcription regulation, transferase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus: Q07794 |
| Total number of polymer chains | 1 |
| Total formula weight | 52747.73 |
| Authors | Yuan, Y.A. (deposition date: 2007-10-12, release date: 2008-09-02, Last modification date: 2024-10-30) |
| Primary citation | Lin, C.,Yuan, Y.A. Structural insights into histone h3 lysine 56 acetylation by rtt109 Structure, 16:1503-1510, 2008 Cited by PubMed Abstract: Histone acetylation plays important roles for the regulation of many fundamental cellular processes. Saccharomyces cerevisiae Rtt109 is an important class of histone acetyltransferases (HATs), which promote genome stability by directly acetylating newly synthesized histone H3 lysine 56 (H3-K56) through an unknown mechanism. Here, we report the crystal structures of Rtt109 at 2.2 A and Rtt109/Acetyl-CoA binary complex at 1.9 A. The structure displays a vise-like topology with mixed three-layered alpha/beta module forming the central module, whose core region resembles the structure of GCN5 HAT domain and P300/CBP HAT domain. Using structural and biochemical analyses, we have discovered the catalytic active site and have identified Asp288 as the deprotonation residue and Lys290 as the autoacetylation residue. We have further proposed the unique H3-K56 anchoring pocket and the potential H3alphaN binding groove. Our work has provided structural insights to understand the acetylation mechanism of H3-K56 by Rtt109. PubMed: 18707894DOI: 10.1016/j.str.2008.07.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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