5XM2

Human N-terminal domain of FACT complex subunit SPT16

Summary for 5XM2

• Entry DOI: 10.2210/pdb5xm2/pdb
• Descriptor: FACT complex subunit SPT16, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: fact subunit, spt16n, histone chaperone, dna damage repair, transcription
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 99240.12

Authors

Xu, S.,Li, H.,Dou, Y.,Chen, Y.,Jiang, H.,Lu, D.,Wang, M.,Su, D. (deposition date: 2017-05-12, release date: 2018-05-16, Last modification date: 2024-03-27)

Primary citation

Jiang, H.,Xu, S.,Chen, Y.,Li, H.,Tian, L.,Zhou, H.,Zhao, Z.,Yang, C.,Zhong, Z.,Cai, G.,Su, D.
The structural basis of human Spt16 N-terminal domain interaction with histone (H3-H4)2tetramer.
Biochem.Biophys.Res.Commun., 508:864-870, 2019

PubMed Abstract: FACT (Facilitates Chromatin Transactions) is a heterodimeric protein complex involved in RNA polymerase II transcription elongation, playing essential roles in chromatin remodeling during transcription, replication, and DNA damage repair. The FACT subunit hSpt16 is essential for nucleosome reorganization. The N-terminal domain of hSpt16 (hSpt16-NTD) was recently described as a histone (H3-H4)-binding domain; however, its mode of interaction remains unknown. In this study, we solved the structure of hSpt16-NTD at 2.19 Å and found that a long-disordered region (hSpt16-LDR), after the main body of hSpt16-NTD, is a novel histone-binding motif. Furthermore, hSpt16-LDR interaction with (H3-H4) is H3 N-terminal tail-independent. Therefore, Spt16-NTD is a histone H3-H4-specific binding domain with a distinct mechanism of interaction between histones and histone chaperones.

PubMed: 30528735
DOI: 10.1016/j.bbrc.2018.11.150

Experimental method

X-RAY DIFFRACTION (2.187 Å)