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PDBsum entry 4qc1
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Transcription
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PDB id
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4qc1
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PDB id:
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| Name: |
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Transcription
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Title:
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Crystal structure of human baz2b bromodomain in complex with an acetylated histone 3 peptide (h3k14ac)
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Structure:
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Bromodomain adjacent to zinc finger domain protein 2b. Chain: a, b. Fragment: unp residues 2062-2166. Synonym: hwalp4. Engineered: yes. Acetylated histone 3 peptide (h3k14ac). Chain: d, e. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: baz2b, kiaa1476. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes
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Resolution:
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1.99Å
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R-factor:
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0.215
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R-free:
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0.256
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Authors:
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C.Tallant,B.Jose,S.Picaud,A.Chaikuad,P.Filippakopoulos,N.Burgess- Brown,F.Von Delft,C.H.Arrowsmith,A.M.Edwards,C.Bountra,S.Knapp, Structural Genomics Consortium (Sgc)
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Key ref:
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C.Tallant
et al.
(2015).
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.
Structure,
23,
80-92.
PubMed id:
DOI:
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Date:
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09-May-14
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Release date:
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21-May-14
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PROCHECK
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Headers
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References
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Q9UIF8
(BAZ2B_HUMAN) -
Bromodomain adjacent to zinc finger domain protein 2B from Homo sapiens
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Seq:
Struc:
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2168 a.a.
106 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Structure
23:80-92
(2015)
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PubMed id:
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Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.
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C.Tallant,
E.Valentini,
O.Fedorov,
L.Overvoorde,
F.M.Ferguson,
P.Filippakopoulos,
D.I.Svergun,
S.Knapp,
A.Ciulli.
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ABSTRACT
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Binding of the chromatin remodeling complex NoRC to RNA complementary to the
rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of
NoRC, is involved in recruitment to rDNA by interactions with promoter-bound
TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize
posttranslational modifications on histones are essential for recruitment of
NoRC to chromatin, but how these reader modules recognize site-specific histone
tails has remained elusive. Here, we report crystal structures of PHD zinc
finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3
and/or H4 histones. PHD finger functions as an independent structural module in
recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4
acetylation marks followed by a key basic residue, KacXXR. Further
low-resolution analyses of PHD-bromodomain modules provide molecular insights
into their trans histone tail recognition, required for nucleosome recruitment
and transcriptional repression of the NoRC complex.
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Links
