Ontology highlight
ABSTRACT:
SUBMITTER: Marciano G
PROVIDER: S-EPMC4741192 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology communications 20160122 Pt 2
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 ...[more]