5E5B

Crystal structure of Human Spt16 N-terminal domain

Summary for 5E5B

• Entry DOI: 10.2210/pdb5e5b/pdb
• Descriptor: FACT complex subunit SPT16 (2 entities in total)
• Functional Keywords: pita-bread, aminopeptidase, chromatin, replication, fact, histone binding module, chromosomal protein, dna damage, dna repair, dna replication, nucleus, transcription, transcription regulation
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : Q9Y5B9
• Total number of polymer chains: 1
• Total formula weight: 48720.10

Authors

Marciano, G.,Huang, D.T. (deposition date: 2015-10-08, release date: 2016-02-10, Last modification date: 2024-01-10)

Primary citation

Marciano, G.,Huang, D.T.
Structure of the human histone chaperone FACT Spt16 N-terminal domain.
Acta Crystallogr.,Sect.F, 72:121-128, 2016

PubMed Abstract: The histone chaperone FACT plays an important role in facilitating nucleosome assembly and disassembly during transcription. FACT is a heterodimeric complex consisting of Spt16 and SSRP1. The N-terminal domain of Spt16 resembles an inactive aminopeptidase. How this domain contributes to the histone chaperone activity of FACT remains elusive. Here, the crystal structure of the N-terminal domain (NTD) of human Spt16 is reported at a resolution of 1.84 Å. The structure adopts an aminopeptidase-like fold similar to those of the Saccharomyces cerevisiae and Schizosaccharomyces pombe Spt16 NTDs. Isothermal titration calorimetry analyses show that human Spt16 NTD binds histones H3/H4 with low-micromolar affinity, suggesting that Spt16 NTD may contribute to histone binding in the FACT complex. Surface-residue conservation and electrostatic analysis reveal a conserved acidic patch that may be involved in histone binding.

PubMed: 26841762
DOI: 10.1107/S2053230X15024565

Experimental method

X-RAY DIFFRACTION (1.84 Å)