7K7V
The X-ray crystal structure of SSR4, an S. pombe chromatin remodelling protein: iodide derivative
Summary for 7K7V
| Entry DOI | 10.2210/pdb7k7v/pdb |
| Descriptor | SWI/SNF and RSC complexes subunit ssr4, GLYCEROL, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | chromatin remodelling, sad phasing, novel structure, gene regulation |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 22822.21 |
| Authors | Peat, T.S.,Newman, J. (deposition date: 2020-09-24, release date: 2020-12-16, Last modification date: 2024-03-06) |
| Primary citation | Newman, J.,Nebl, T.,Van, H.,Peat, T.S. The X-ray crystal structure of the N-terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin-remodelling protein. Acta Crystallogr.,Sect.F, 76:583-589, 2020 Cited by PubMed Abstract: Ssr4 is a yeast protein from Schizosaccharomyces pombe and is an essential part of the chromatin-remodelling [SWI/SNF and RSC (remodelling the structure of chromatin)] complexes found in S. pombe. These complexes (or their homologues) regulate gene expression in eukaryotic organisms, affecting a large number of genes both positively and negatively. The downstream effects are seen in development, and in humans have implications for disease such as cancer. The chromatin structure is altered by modifying the DNA-histone contacts, thus opening up or closing down sections of DNA to specific transcription factors that regulate the transcription of genes. The Ssr4 sequence has little homology to other sequences in the Protein Data Bank, so the structure was solved using an iodine derivative with SAD phasing. The structure of the N-terminal domain is an antiparallel β-sheet of seven strands with α-helices on one side and random coil on the other. The structure is significantly different to deposited structures and was used as a target in the most recent Critical Assessment of Techniques for Protein Structure Prediction (CASP; https://predictioncenter.org/) competition. PubMed: 33263569DOI: 10.1107/S2053230X20015216 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.882 Å) |
Structure validation
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