6W4L

The crystal structure of a single chain H2B-H2A histone chimera from Xenopus laevis

6W4L の概要

• エントリーDOI: 10.2210/pdb6w4l/pdb
• 分子名称: Histone H2B 1.1,Histone H2A type 1, PYROPHOSPHATE (3 entities in total)
• 機能のキーワード: histone, chromatin, gene regulation
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20699.68

構造登録者

Warren, C.,Bonanno, J.B.,Almo, S.C.,Shechter, D. (登録日: 2020-03-11, 公開日: 2020-05-06, 最終更新日: 2023-10-18)

主引用文献

Warren, C.,Bonanno, J.B.,Almo, S.C.,Shechter, D.
Structure of a single-chain H2A/H2B dimer.
Acta Crystallogr.,Sect.F, 76:194-198, 2020

PubMed Abstract: Chromatin is the complex assembly of nucleic acids and proteins that makes up the physiological form of the eukaryotic genome. The nucleosome is the fundamental repeating unit of chromatin, and is composed of ∼147 bp of DNA wrapped around a histone octamer formed by two copies of each core histone: H2A, H2B, H3 and H4. Prior to nucleosome assembly, and during histone eviction, histones are typically assembled into soluble H2A/H2B dimers and H3/H4 dimers and tetramers. A multitude of factors interact with soluble histone dimers and tetramers, including chaperones, importins, histone-modifying enzymes and chromatin-remodeling enzymes. It is still unclear how many of these proteins recognize soluble histones; therefore, there is a need for new structural tools to study non-nucleosomal histones. Here, a single-chain, tailless Xenopus H2A/H2B dimer was created by directly fusing the C-terminus of H2B to the N-terminus of H2A. It is shown that this construct (termed scH2BH2A) is readily expressed in bacteria and can be purified under non-denaturing conditions. A 1.31 Å resolution crystal structure of scH2BH2A shows that it adopts a conformation that is nearly identical to that of nucleosomal H2A/H2B. This new tool is likely to facilitate future structural studies of many H2A/H2B-interacting proteins.

PubMed: 32356520
DOI: 10.1107/S2053230X20004604

実験手法

X-RAY DIFFRACTION (1.31 Å)