The X‐ray crystal structure of the N‐terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin‐remodelling protein. Issue 12 (4th December 2020)

• Record Type: Journal Article
• Authors: Newman, Janet; Nebl, Tom; Van, Huy; Peat, Thomas S.
• Is Part Of: Acta crystallographica. Volume 76:Issue 12(2020:Dec.)
• Page Start: 583
• Page End: 589
• Publication Date: 2020-12-04
• Subjects: chromatin remodelling -- SAD phasing -- novel structure -- Schizosaccharomyces pombe; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X20015216
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The N‐terminal domain of Ssr4 from S. pombe, which is an integral protein in the SWI/SNF and RSC chromatin‐remodelling complexes, has been crystallized and its structure has been solved using iodine as a phasing vehicle. 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.