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PDBsum entry 4l7x

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protein ligands metals links
Cell cycle, gene regulation PDB id
4l7x

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
58 a.a.
Ligands
ALA-ARG-THR-M3L-
GLN-THR-ALA
Metals
_ZN ×2
Waters ×74
PDB id:
4l7x
Name: Cell cycle, gene regulation
Title: Crystal structure of the dido phd finger in complex with h3k4me3
Structure: Death-inducer obliterator 1. Chain: a. Fragment: phd-type zinc finger domain residues 266-325. Synonym: dio-1, hdido1, death-associated transcription factor 1, datf-1. Engineered: yes. Histone h3 peptide. Chain: u. Synonym: h3k4me3 peptide.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dido1, c20orf158, datf1, kiaa0333. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: peptide was synthesized.
Resolution:
1.35Å     R-factor:   0.133     R-free:   0.142
Authors: Q.Tong,J.Gatchalian,T.G.Kutateladze
Key ref: J.Gatchalian et al. (2013). Dido3 PHD modulates cell differentiation and division. Cell Rep, 4, 148-158. PubMed id: 23831028 DOI: 10.1016/j.celrep.2013.06.014
Date:
14-Jun-13     Release date:   24-Jul-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9BTC0  (DIDO1_HUMAN) -  Death-inducer obliterator 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2240 a.a.
58 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1016/j.celrep.2013.06.014 Cell Rep 4:148-158 (2013)
PubMed id: 23831028  
 
 
Dido3 PHD modulates cell differentiation and division.
J.Gatchalian, A.Fütterer, S.B.Rothbart, Q.Tong, H.Rincon-Arano, A.Sánchez de Diego, M.Groudine, B.D.Strahl, C.Martínez-A, K.H.van Wely, T.G.Kutateladze.
 
  ABSTRACT  
 
Death Inducer Obliterator 3 (Dido3) is implicated in the maintenance of stem cell genomic stability and tumorigenesis. Here, we show that Dido3 regulates the expression of stemness genes in embryonic stem cells through its plant homeodomain (PHD) finger. Binding of Dido3 PHD to histone H3K4me3 is disrupted by threonine phosphorylation that triggers Dido3 translocation from chromatin to the mitotic spindle. The crystal structure of Dido3 PHD in complex with H3K4me3 reveals an atypical aromatic-cage-like binding site that contains a histidine residue. Biochemical, structural, and mutational analyses of the binding mechanism identified the determinants of specificity and affinity and explained the inability of homologous PHF3 to bind H3K4me3. Together, our findings reveal a link between the transcriptional control in embryonic development and regulation of cell division.
 

 

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