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Transcription PDB id
1pzw
Jmol
Contents
Protein chain
80 a.a. *
Metals
_ZN
Waters ×56
* Residue conservation analysis
PDB id:
1pzw
Name: Transcription
Title: Crystal structure of the zinc finger associated domain of th drosophila transcription factor grauzone
Structure: Transcription factor grauzone. Chain: a. Fragment: zinc finger associated domain (zad). Synonym: zinc finger associated domain of drosophila grauzo grauzone cg33133-pa. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: grauzone. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.242     R-free:   0.267
Authors: R.Jauch,G.P.Bourenkov,H.-R.Chung,H.Urlaub,U.Reidt,H.Jaeckle,
Key ref:
R.Jauch et al. (2003). The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module. Structure, 11, 1393-1402. PubMed id: 14604529 DOI: 10.1016/j.str.2003.09.015
Date:
14-Jul-03     Release date:   04-Nov-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9U405  (GRAU_DROME) -  Transcription factor grauzone
Seq:
Struc:
 
Seq:
Struc:
570 a.a.
80 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biochemical function     zinc ion binding     1 term  

 

 
DOI no: 10.1016/j.str.2003.09.015 Structure 11:1393-1402 (2003)
PubMed id: 14604529  
 
 
The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module.
R.Jauch, G.P.Bourenkov, H.R.Chung, H.Urlaub, U.Reidt, H.Jäckle, M.C.Wahl.
 
  ABSTRACT  
 
About one-third of the more than 300 C2H2 zinc finger proteins of Drosophila contain a conserved sequence motif, the zinc finger-associated domain (ZAD). Genes that encode ZAD proteins are specific for and expanded in the genomes of insects. Only three ZAD-encoding gene functions are established, and the role of ZAD is unknown. Here we present the crystal structure of the ZAD of Grauzone (ZAD(Grau)), a Drosophila transcription factor that specifically controls the maternal Cdc20-like APC subunit Cortex. ZAD forms an atypical treble-clef-like zinc-coordinating fold. Head-to-tail arrangement of two ZAD(Grau) molecules in the crystals suggests dimer formation, an observation supported by crosslinking and dynamic light scattering. The results indicate that ZAD provides a novel protein-protein interaction module that characterizes a large family of insect transcription factors.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. The ZAD[Grau] Dimer(A) Stereo ribbon plot of a ZAD[Grau] dimer as seen in the crystal. The two subunits (Mol I and Mol II) are colored red and blue; the two zinc centers are depicted in ball-and-stick. N- and C termini are labeled. The orientation of the rear subunit is the same as in Figure 2A.(B) Stereo representation of residue interactions in the dimer interface, 90° from the view in (A). The two ZAD[Grau] subunits are colored as in (A) but are rendered semitransparent to clearly reveal the interacting residues in ball-and-stick. All residues and the molecular termini are labeled.(C) Mapping of the contact residues within the dimer (green) onto the surface of a ZAD[Grau] monomer (gray). The orientation of the molecule is the same as that of the red subunit in (A).(D) Mapping in orange of conserved residues on the surface of ZAD[Grau] in two diametric views. The left orientation is the same as in (C), indicating that the largest conserved surface patch and the dimer interface largely coincide.
 
  The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1393-1402) copyright 2003.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20045686 J.P.Lewandowski, K.B.Sheehan, P.E.Bennett, and R.E.Boswell (2010).
Mago Nashi, Tsunagi/Y14, and Ranshi form a complex that influences oocyte differentiation in Drosophila melanogaster.
  Dev Biol, 339, 307-319.  
19530132 L.Aravind, V.Anantharaman, and T.M.Venancio (2009).
Apprehending multicellularity: regulatory networks, genomics, and evolutiony.
  Birth Defects Res C Embryo Today, 87, 143-164.  
18073205 D.Bessière, C.Lacroix, S.Campagne, V.Ecochard, V.Guillet, L.Mourey, F.Lopez, J.Czaplicki, P.Demange, A.Milon, J.P.Girard, and V.Gervais (2008).
Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways.
  J Biol Chem, 283, 4352-4363.
PDB code: 2jtg
16216586 R.Jauch, S.Jäkel, C.Netter, K.Schreiter, B.Aicher, H.Jäckle, and M.C.Wahl (2005).
Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site.
  Structure, 13, 1559-1568.
PDB codes: 2ac3 2ac5
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.