9B1D

Cryo-EM structure of native SWR1 bound to DNA (composite structure)

This is a non-PDB format compatible entry.

Summary for 9B1D

• Entry DOI: 10.2210/pdb9b1d/pdb
• EMDB information: 44074 44110
• Descriptor: Helicase SWR1, MAGNESIUM ION, ZINC ION, ... (12 entities in total)
• Functional Keywords: chromatin remodeler, snf2 family atpase, histone exchange, h2a.z, gene regulation
• Biological source: Saccharomyces cerevisiae W303; More
• Total number of polymer chains: 12
• Total formula weight: 875078.28

Authors

Louder, R.K.,Park, G.,Wu, C. (deposition date: 2024-03-13, release date: 2024-10-09, Last modification date: 2024-12-11)

Primary citation

Louder, R.K.,Park, G.,Ye, Z.,Cha, J.S.,Gardner, A.M.,Lei, Q.,Ranjan, A.,Hollmuller, E.,Stengel, F.,Pugh, B.F.,Wu, C.
Molecular basis of global promoter sensing and nucleosome capture by the SWR1 chromatin remodeler.
Cell, 187:6849-6864.e18, 2024

PubMed Abstract: The SWR1 chromatin remodeling complex is recruited to +1 nucleosomes downstream of transcription start sites of eukaryotic promoters, where it exchanges histone H2A for the specialized variant H2A.Z. Here, we use cryoelectron microscopy (cryo-EM) to resolve the structural basis of the SWR1 interaction with free DNA, revealing a distinct open conformation of the Swr1 ATPase that enables sliding from accessible DNA to nucleosomes. A complete structural model of the SWR1-nucleosome complex illustrates critical roles for Swc2 and Swc3 subunits in oriented nucleosome engagement by SWR1. Moreover, an extended DNA-binding α helix within the Swc3 subunit enables sensing of nucleosome linker length and is essential for SWR1-promoter-specific recruitment and activity. The previously unresolved N-SWR1 subcomplex forms a flexible extended structure, enabling multivalent recognition of acetylated histone tails by reader domains to further direct SWR1 toward the +1 nucleosome. Altogether, our findings provide a generalizable mechanism for promoter-specific targeting of chromatin and transcription complexes.

PubMed: 39357520
DOI: 10.1016/j.cell.2024.09.007

Experimental method

ELECTRON MICROSCOPY (3.3 Å)