8I17

Structural basis for H2A-H2B recognitions by human Spt16

Summary for 8I17

• Entry DOI: 10.2210/pdb8i17/pdb
• Descriptor: Histone H2A type 1-B/E, Histone H2B type 1-J, FACT complex subunit SPT16, ... (5 entities in total)
• Functional Keywords: histone chaperone, histone, chaperone
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 9
• Total formula weight: 80882.08

Authors

Huang, H.,Li, Y. (deposition date: 2023-01-12, release date: 2023-02-22, Last modification date: 2024-05-29)

Primary citation

Li, Y.,Huang, H.
Structural basis for H2A-H2B recognitions by human Spt16.
Biochem.Biophys.Res.Commun., 651:85-91, 2023

PubMed Abstract: The human facilitates chromatin transcription (FACT) complex, consisting of Spt16 and SSRP1, is a versatile histone chaperone that can engage free H2A-H2B dimer and H3-H4 tetramer (or dimer), and partially unraveled nucleosome. The C-terminal domain of human Spt16 (hSpt16-CTD) is the decisive element for engaging H2A-H2B dimer and partially unraveled nucleosome. The molecular basis of the H2A-H2B dimer recognitions by hSpt16-CTD is not fully comprehended. Here, we present a high-resolution snapshot of the recognitions of the H2A-H2B dimer by hSpt16-CTD via an acidic intrinsically disordered (AID) segment, and reveal some distinct structural features of hSpt16-CTD as compared to the budding yeast Spt16-CTD.

PubMed: 36801613
DOI: 10.1016/j.bbrc.2023.02.016

Experimental method

X-RAY DIFFRACTION (1.98 Å)