4BB7

Crystal structure of the yeast Rsc2 BAH domain

Summary for 4BB7

• Entry DOI: 10.2210/pdb4bb7/pdb
• Descriptor: CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC2, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: transcription, dna binding
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: Q06488
• Total number of polymer chains: 4
• Total formula weight: 121564.69

Authors

Chambers, A.L.,Pearl, L.H.,Oliver, A.W.,Downs, J.A. (deposition date: 2012-09-20, release date: 2013-08-14, Last modification date: 2023-12-20)

Primary citation

Chambers, A.L.,Pearl, L.H.,Oliver, A.W.,Downs, J.A.
The Bah Domain of Rsc2 is a Histone H3 Binding Domain.
Nucleic Acids Res., 41:9168-, 2013

PubMed Abstract: Bromo-adjacent homology (BAH) domains are commonly found in chromatin-associated proteins and fall into two classes; Remodels the Structure of Chromatin (RSC)-like or Sir3-like. Although Sir3-like BAH domains bind nucleosomes, the binding partners of RSC-like BAH domains are currently unknown. The Rsc2 subunit of the RSC chromatin remodeling complex contains an RSC-like BAH domain and, like the Sir3-like BAH domains, we find Rsc2 BAH also interacts with nucleosomes. However, unlike Sir3-like BAH domains, we find that Rsc2 BAH can bind to recombinant purified H3 in vitro, suggesting that the mechanism of nucleosome binding is not conserved. To gain insight into the Rsc2 BAH domain, we determined its crystal structure at 2.4 Å resolution. We find that it differs substantially from Sir3-like BAH domains and lacks the motifs in these domains known to be critical for making contacts with histones. We then go on to identify a novel motif in Rsc2 BAH that is critical for efficient H3 binding in vitro and show that mutation of this motif results in defective Rsc2 function in vivo. Moreover, we find this interaction is conserved across Rsc2-related proteins. These data uncover a binding target of the Rsc2 family of BAH domains and identify a novel motif that mediates this interaction.

PubMed: 23907388
DOI: 10.1093/NAR/GKT662

Experimental method

X-RAY DIFFRACTION (2.4 Å)