PDBsum entry 3coq

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protein dna_rna ligands metals Protein-protein interface(s) links
Transcription/DNA PDB id
Protein chains
89 a.a. *
_ZN ×4
Waters ×33
* Residue conservation analysis
PDB id:
Name: Transcription/DNA
Title: Structural basis for dimerization in DNA recognition by gal4
Structure: Regulatory protein gal4. Chain: a, b. Fragment: DNA binding domain with complete dimerization dom engineered: yes. DNA (5'- d( Dap Dcp Dcp Dgp Dgp Dap Dgp Dgp Dap Dcp Dap Dgp Dtp Dcp P Dcp Dgp Dg)-3'). Chain: d. Engineered: yes.
Source: Saccharomyces cerevisiae. Baker's yeast. Gene: gal4. Expressed in: escherichia coli. Synthetic: yes. Synthetic: yes
2.40Å     R-factor:   0.213     R-free:   0.269
Authors: M.Hong,M.X.Fitzgerald,S.Harper,C.Luo,D.W.Speicher
Key ref: M.Hong et al. (2008). Structural basis for dimerization in DNA recognition by Gal4. Structure, 16, 1019-1026. PubMed id: 18611375
29-Mar-08     Release date:   01-Jul-08    
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Protein chains
No UniProt id for this chain
Struc: 89 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     sequence-specific DNA binding RNA polymerase II transcription factor activity     2 terms  


Structure 16:1019-1026 (2008)
PubMed id: 18611375  
Structural basis for dimerization in DNA recognition by Gal4.
M.Hong, M.X.Fitzgerald, S.Harper, C.Luo, D.W.Speicher, R.Marmorstein.
Gal4 is a Zn2Cys6 binuclear cluster containing transcription factor that binds DNA as a homodimer and can activate transcription by interacting with the mutant Gal11P protein. Although structures have been reported of the Gal4 dimerization domain and the binuclear cluster domain bound to DNA as a dimer, the structure of the "complete" Gal4 dimer bound to DNA has not previously been described. Here we report the structure of a complete Gal4 dimer bound to DNA and additional biochemical studies to address the molecular basis for Gal4 dimerization in DNA binding. We find that Gal4 dimerization on DNA is mediated by an intertwined helical bundle that deviates significantly from the solution NMR structure of the free dimerization domain. Associated biochemical studies show that the dimerization domain of Gal4 is important for DNA binding and protein thermostability. We also map the interaction surface of the Gal4 dimerization domain with Gal11P.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20953181 M.D.Daugherty, B.Liu, and A.D.Frankel (2010).
Structural basis for cooperative RNA binding and export complex assembly by HIV Rev.
  Nat Struct Mol Biol, 17, 1337-1342.
PDB code: 3lph
20434983 M.Floer, X.Wang, V.Prabhu, G.Berrozpe, S.Narayan, D.Spagna, D.Alvarez, J.Kendall, A.Krasnitz, A.Stepansky, J.Hicks, G.O.Bryant, and M.Ptashne (2010).
A RSC/nucleosome complex determines chromatin architecture and facilitates activator binding.
  Cell, 141, 407-418.  
19380488 H.Murakami, and A.Nicolas (2009).
Locally, meiotic double-strand breaks targeted by Gal4BD-Spo11 occur at discrete sites with a sequence preference.
  Mol Cell Biol, 29, 3500-3516.  
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