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PDBsum entry 5e5b
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Transcription
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PDB id
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5e5b
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PDB id:
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Transcription
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Title:
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Crystal structure of human spt16 n-terminal domain
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Structure:
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Fact complex subunit spt16. Chain: a. Fragment: n-terminal fragment, residues 1-510. 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: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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1.84Å
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R-factor:
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0.157
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R-free:
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0.176
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Authors:
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G.Marciano,D.T.Huang
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Key ref:
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G.Marcianò
and
D.T.Huang
(2016).
Structure of the human histone chaperone FACT Spt16 N-terminal domain.
Acta Crystallogr F Struct Biol Commun,
72,
121-128.
PubMed id:
DOI:
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Date:
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08-Oct-15
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Release date:
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10-Feb-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.
431 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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Acta Crystallogr F Struct Biol Commun
72:121-128
(2016)
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PubMed id:
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Structure of the human histone chaperone FACT Spt16 N-terminal domain.
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G.Marcianò,
D.T.Huang.
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ABSTRACT
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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.
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