5CHL

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex

5CHL の概要

• エントリーDOI: 10.2210/pdb5chl/pdb
• 分子名称: Vacuolar protein sorting-associated protein 72 homolog, Histone H2A.Z (3 entities in total)
• 機能のキーワード: remodeling complex, histone, chaperone
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Nucleus : Q9VKM6 P0C0S5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29747.11

構造登録者

Shan, S.,Liang, X.,Pan, L.,Wu, C.,Zhou, Z. (登録日: 2015-07-10, 公開日: 2016-03-09, 最終更新日: 2024-11-20)

主引用文献

Liang, X.,Shan, S.,Pan, L.,Zhao, J.,Ranjan, A.,Wang, F.,Zhang, Z.,Huang, Y.,Feng, H.,Wei, D.,Huang, L.,Liu, X.,Zhong, Q.,Lou, J.,Li, G.,Wu, C.,Zhou, Z.
Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1
Nat.Struct.Mol.Biol., 23:317-323, 2016

PubMed Abstract: Histone variant H2A.Z, a universal mark of dynamic nucleosomes flanking gene promoters and enhancers, is incorporated into chromatin by SRCAP (SWR1), an ATP-dependent, multicomponent chromatin-remodeling complex. The YL1 (Swc2) subunit of SRCAP (SWR1) plays an essential role in H2A.Z recognition, but how it achieves this has been unclear. Here, we report the crystal structure of the H2A.Z-binding domain of Drosophila melanogaster YL1 (dYL1-Z) in complex with an H2A.Z-H2B dimer at 1.9-Å resolution. The dYL1-Z domain adopts a new whip-like structure that wraps over H2A.Z-H2B, and preferential recognition is largely conferred by three residues in loop 2, the hyperacidic patch and the extended αC helix of H2A.Z. Importantly, this domain is essential for deposition of budding yeast H2A.Z in vivo and SRCAP (SWR1)-catalyzed histone H2A.Z replacement in vitro. Our studies distinguish YL1-Z from known H2A.Z chaperones and suggest a hierarchical mechanism based on increasing binding affinity facilitating H2A.Z transfer from SRCAP (SWR1) to the nucleosome.

PubMed: 26974124
DOI: 10.1038/nsmb.3190

実験手法

X-RAY DIFFRACTION (1.892 Å)