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PDBsum entry 6t7b

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protein dna_rna Protein-protein interface(s) links
Nuclear protein PDB id
6t7b

 

 

 

 

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Contents
Protein chains
98 a.a.
84 a.a.
106 a.a.
95 a.a.
76 a.a.
DNA/RNA
PDB id:
6t7b
Name: Nuclear protein
Title: Structure of human sox2 transcription factor in complex with a nucleosome
Structure: Histone h3.2. Chain: a, e. Synonym: histone h3/m,histone h3/o. Engineered: yes. Histone h4. Chain: b, f. Engineered: yes. Histone h2a type 1-b/e. Chain: c, g.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hist2h3a, hist2h3c, h3f2, h3fm, hist2h3d. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hist1h4a, h4/a, h4fa, hist1h4b, h4/i, h4fi, hist1h4c, h4/g, h4fg, hist1h4d, h4/b, h4fb, hist1h4e, h4/j, h4fj, hist1h4f, h4/c, h4fc, hist1h4h, h4/h, h4fh, hist1h4i, h4/m, h4fm, hist1h4j, h4/e,
Authors: S.O.Dodonova,F.Zhu,C.Dienemann,J.Taipale,P.Cramer
Key ref: S.O.Dodonova et al. (2020). Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function. Nature, 580, 669-672. PubMed id: 32350470 DOI: 10.1038/s41586-020-2195-y
Date:
21-Oct-19     Release date:   29-Apr-20    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q71DI3  (H32_HUMAN) -  Histone H3.2 from Homo sapiens
Seq:
Struc:
136 a.a.
98 a.a.*
Protein chains
Pfam   ArchSchema ?
P62805  (H4_HUMAN) -  Histone H4 from Homo sapiens
Seq:
Struc:
103 a.a.
84 a.a.
Protein chains
Pfam   ArchSchema ?
P04908  (H2A1B_HUMAN) -  Histone H2A type 1-B/E from Homo sapiens
Seq:
Struc:
130 a.a.
106 a.a.
Protein chains
Pfam   ArchSchema ?
O60814  (H2B1K_HUMAN) -  Histone H2B type 1-K from Homo sapiens
Seq:
Struc:
126 a.a.
95 a.a.
Protein chain
Pfam   ArchSchema ?
P48431  (SOX2_HUMAN) -  Transcription factor SOX-2 from Homo sapiens
Seq:
Struc:
317 a.a.
76 a.a.
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

DNA/RNA chains
  C-T-A-A-T-T-T-A-T-G-T-T-T-G-T-T-A-G-C-G-T-T-A-T-A-C-T-A-T-T-C-T-A-A-T-T-C-T-T- 95 bases
  C-G-T-T-A-G-G-C-A-T-T-A-A-G-C-T-G-A-A-C-G-C-A-C-A-A-A-G-G-A-A-C-A-A-A-A-T-A-A- 95 bases

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H, K: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/s41586-020-2195-y Nature 580:669-672 (2020)
PubMed id: 32350470  
 
 
Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.
S.O.Dodonova, F.Zhu, C.Dienemann, J.Taipale, P.Cramer.
 
  ABSTRACT  
 
'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming1,2. Pioneer factors can bind nucleosomal DNA to enable gene expression from regions of the genome with closed chromatin. SOX2 is a prominent pioneer factor that is essential for pluripotency and self-renewal of embryonic stem cells3. Here we report cryo-electron microscopy structures of the DNA-binding domains of SOX2 and its close homologue SOX11 bound to nucleosomes. The structures show that SOX factors can bind and locally distort DNA at superhelical location 2. The factors also facilitate detachment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility. SOX-factor binding to the nucleosome can also lead to a repositioning of the N-terminal tail of histone H4 that includes residue lysine 16. We speculate that this repositioning is incompatible with higher-order nucleosome stacking, which involves contacts of the H4 tail with a neighbouring nucleosome. Our results indicate that pioneer transcription factors can use binding energy to initiate chromatin opening, and thereby facilitate nucleosome remodelling and subsequent transcription.
 

 

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