6A7U

Crystal structure of histone H2A.Bbd-H2B dimer

Summary for 6A7U

• Entry DOI: 10.2210/pdb6a7u/pdb
• Descriptor: Histone H2B type 2-E,Histone H2A-Bbd type 2/3 (2 entities in total)
• Functional Keywords: histone, histone variant, h2a.bbd, dna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 26534.45

Authors

Dai, L.,Zhou, Z. (deposition date: 2018-07-04, release date: 2019-02-27, Last modification date: 2023-11-22)

Primary citation

Dai, L.,Xie, X.,Zhou, Z.
Crystal structure of the histone heterodimer containing histone variant H2A.Bbd.
Biochem. Biophys. Res. Commun., 503:1786-1791, 2018

PubMed Abstract: H2A.Bbd, the most divergent histone variant among all known H2A type histones, is involved in gene transcription, spermiogenesis, DNA replication and RNA splicing. Incorporation of H2A.Bbd-H2B dimer, a fundamental unit of H2A.Bbd nucleosome, modulate structures of nucleosome or chromatin, but the underlying mechanism remains elusive. Here we determined a crystal structure of H2A.Bbd-H2B dimer at 2.6 Å resolution. Although the H2A.Bbd-H2B dimer structure largely resembles that of H2A-H2B, substitution of H2A αC helix residues by H2A.Bbd counterparts lead to the transition of a long αC-helix to the short 3-helix, likely owing to the rearrangement of the hydrogen-bond network. Moreover, structural comparison revealed a strikingly altered electrostatic potential surface for H2A.Bbd-H2B dimer displaying a diminished DNA binding capability. Our study provides the first high-resolution structure of histone variant H2A.Bbd and shed a light on biological function of H2A.Bbd.

PubMed: 30064909
DOI: 10.1016/j.bbrc.2018.07.114

Experimental method

X-RAY DIFFRACTION (2.6 Å)