4M6B

Crystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimer

Summary for 4M6B

• Entry DOI: 10.2210/pdb4m6b/pdb
• Descriptor: Chimera protein of Histone H2B.1 and Histone H2A.Z, Helicase SWR1 (3 entities in total)
• Functional Keywords: chromatin remodeler, histone binding, structural protein-hydrolase complex, structural protein/hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus : Q12692 Q05471
• Total number of polymer chains: 4
• Total formula weight: 54351.13

Authors

Hong, J.J.,Feng, H.Q.,Wang, F.,Ranjan, A.,Chen, J.H.,Jiang, J.S.,Girlando, R.,Xiao, T.S.,Wu, C.,Bai, Y.W. (deposition date: 2013-08-09, release date: 2014-02-19, Last modification date: 2024-02-28)

Primary citation

Hong, J.,Feng, H.,Wang, F.,Ranjan, A.,Chen, J.,Jiang, J.,Ghirlando, R.,Xiao, T.S.,Wu, C.,Bai, Y.
The Catalytic Subunit of the SWR1 Remodeler Is a Histone Chaperone for the H2A.Z-H2B Dimer.
Mol.Cell, 53:498-505, 2014

PubMed Abstract: Histone variant H2A.Z-containing nucleosomes exist at most eukaryotic promoters and play important roles in gene transcription and genome stability. The multisubunit nucleosome-remodeling enzyme complex SWR1, conserved from yeast to mammals, catalyzes the ATP-dependent replacement of histone H2A in canonical nucleosomes with H2A.Z. How SWR1 catalyzes the replacement reaction is largely unknown. Here, we determined the crystal structure of the N-terminal region (599-627) of the catalytic subunit Swr1, termed Swr1-Z domain, in complex with the H2A.Z-H2B dimer at 1.78 Å resolution. The Swr1-Z domain forms a 310 helix and an irregular chain. A conserved LxxLF motif in the Swr1-Z 310 helix specifically recognizes the αC helix of H2A.Z. Our results show that the Swr1-Z domain can deliver the H2A.Z-H2B dimer to the DNA-(H3-H4)2 tetrasome to form the nucleosome by a histone chaperone mechanism.

PubMed: 24507717
DOI: 10.1016/j.molcel.2014.01.010

Experimental method

X-RAY DIFFRACTION (1.78 Å)