5T5K

Structure of histone-based chromatin in Archaea

Summary for 5T5K

• Entry DOI: 10.2210/pdb5t5k/pdb
• Descriptor: DNA-binding protein HMf-2, DNA (90-MER), CACODYLATE ION, ... (4 entities in total)
• Functional Keywords: nucleosome, chromatin, archaea histones, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Methanothermus fervidus; More
• Total number of polymer chains: 8
• Total formula weight: 102025.84

Authors

Bhattacharyya, S.,Mattiroli, F.,Dyer, P.N.,Sandman, K.,Reeve, J.N.,Luger, K. (deposition date: 2016-08-31, release date: 2017-08-23, Last modification date: 2023-10-04)

Primary citation

Mattiroli, F.,Bhattacharyya, S.,Dyer, P.N.,White, A.E.,Sandman, K.,Burkhart, B.W.,Byrne, K.R.,Lee, T.,Ahn, N.G.,Santangelo, T.J.,Reeve, J.N.,Luger, K.
Structure of histone-based chromatin in Archaea.
Science, 357:609-612, 2017

PubMed Abstract: Small basic proteins present in most Archaea share a common ancestor with the eukaryotic core histones. We report the crystal structure of an archaeal histone-DNA complex. DNA wraps around an extended polymer, formed by archaeal histone homodimers, in a quasi-continuous superhelix with the same geometry as DNA in the eukaryotic nucleosome. Substitutions of a conserved glycine at the interface of adjacent protein layers destabilize archaeal chromatin, reduce growth rate, and impair transcription regulation, confirming the biological importance of the polymeric structure. Our data establish that the histone-based mechanism of DNA compaction predates the nucleosome, illuminating the origin of the nucleosome.

PubMed: 28798133
DOI: 10.1126/science.aaj1849

Experimental method

X-RAY DIFFRACTION (4 Å)