2RSD
Solution structure of the plant homeodomain (PHD) of the E3 SUMO ligase Siz1 from rice
Summary for 2RSD
| Entry DOI | 10.2210/pdb2rsd/pdb |
| NMR Information | BMRB: 11469 |
| Descriptor | E3 SUMO-protein ligase SIZ1, ZINC ION (2 entities in total) |
| Functional Keywords | e3 sumo ligase, plant homeodomain (phd), histone binding, ligase |
| Biological source | Oryza sativa Japonica Group (Japanese rice) |
| Cellular location | Nucleus (By similarity): Q6L4L4 |
| Total number of polymer chains | 1 |
| Total formula weight | 7802.54 |
| Authors | Shindo, H.,Tsuchiya, W.,Suzuki, R.,Yamazaki, T. (deposition date: 2012-01-12, release date: 2012-08-15, Last modification date: 2024-05-15) |
| Primary citation | Shindo, H.,Suzuki, R.,Tsuchiya, W.,Taichi, M.,Nishiuchi, Y.,Yamazaki, T. PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2 Febs Lett., 586:1783-1789, 2012 Cited by PubMed Abstract: We determined the three-dimensional structure of the PHD finger of the rice Siz/PIAS-type SUMO ligase, OsSiz1, by NMR spectroscopy and investigated binding ability for a variety of methylated histone H3 tails, showing that OsSiz1-PHD primarily recognizes dimethylated Arg2 of the histone H3 and that methylations at Arg2 and Lys4 reveal synergy effect on binding to OsSiz1-PHD. The K4 cage of OsSiz1-PHD for trimethylated Lys4 of H3K4me3 was similar to that of the BPTF-PHD finger, while the R2 pocket for Arg2 was different. It is intriguing that the PHD module of Siz/PIAS plays an important role, with collaboration with the DNA binding domain SAP, in gene regulation through SUMOylation of a variety of effectors associated with the methylated arginine-riched chromatin domains. PubMed: 22626555DOI: 10.1016/j.febslet.2012.04.063 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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