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PDBsum entry 4z2n
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Transcription
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PDB id
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4z2n
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PDB id:
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Transcription
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Title:
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Crystal structure of human fact spt16 middle domain
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Structure:
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Fact complex subunit spt16. Chain: a. Fragment: unp residues 644-930. Synonym: chromatin-specific transcription elongation factor 140 kda subunit,fact 140 kda subunit,factp140,facilitates chromatin transcription complex subunit spt16,hspt16. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: supt16h, fact140, factp140. Expressed in: baculovirus expression vector pfastbac1-hm. Expression_system_taxid: 274590
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Resolution:
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1.92Å
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R-factor:
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0.178
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R-free:
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0.216
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Authors:
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Y.Tsunaka,Y.Fujiwara,T.Oyama,S.Hirose,K.Morikawa
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Key ref:
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Y.Tsunaka
et al.
(2016).
Integrated molecular mechanism directing nucleosome reorganization by human FACT.
Genes Dev,
30,
673-686.
PubMed id:
DOI:
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Date:
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30-Mar-15
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Release date:
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09-Mar-16
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PROCHECK
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Headers
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References
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Q9Y5B9
(SP16H_HUMAN) -
FACT complex subunit SPT16 from Homo sapiens
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Seq:
Struc:
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1047 a.a.
268 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Genes Dev
30:673-686
(2016)
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PubMed id:
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Integrated molecular mechanism directing nucleosome reorganization by human FACT.
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Y.Tsunaka,
Y.Fujiwara,
T.Oyama,
S.Hirose,
K.Morikawa.
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ABSTRACT
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Facilitates chromatin transcription (FACT) plays essential roles in chromatin
remodeling during DNA transcription, replication, and repair. Our structural and
biochemical studies of human FACT-histone interactions present precise views of
nucleosome reorganization, conducted by the FACT-SPT16 (suppressor of Ty 16) Mid
domain and its adjacent acidic AID segment. AID accesses the H2B N-terminal
basic region exposed by partial unwrapping of the nucleosomal DNA, thereby
triggering the invasion of FACT into the nucleosome. The crystal structure of
the Mid domain complexed with an H3-H4 tetramer exhibits two separate contact
sites; the Mid domain forms a novel intermolecular β structure with H4. At the
other site, the Mid-H2A steric collision on the H2A-docking surface of the H3-H4
tetramer within the nucleosome induces H2A-H2B displacement. This integrated
mechanism results in disrupting the H3 αN helix, which is essential for
retaining the nucleosomal DNA ends, and hence facilitates DNA stripping from
histone.
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Links
