1PZW

Crystal structure of the zinc finger associated domain of the Drosophila transcription factor Grauzone

Summary for 1PZW

• Entry DOI: 10.2210/pdb1pzw/pdb
• Descriptor: Transcription factor grauzone, ZINC ION (3 entities in total)
• Functional Keywords: dimerization, transcription regulation, treble-clef zinc finger, zad, transcription
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 9232.83

Authors

Jauch, R.,Bourenkov, G.P.,Chung, H.-R.,Urlaub, H.,Reidt, U.,Jaeckle, H.,Wahl, M.C. (deposition date: 2003-07-14, release date: 2003-11-04, Last modification date: 2024-02-14)

Primary citation

Jauch, R.,Bourenkov, G.P.,Chung, H.-R.,Urlaub, H.,Reidt, U.,Wahl, M.C.
The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module
STRUCTURE, 11:1393-1402, 2003

PubMed 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.

PubMed: 14604529
DOI: 10.1016/j.str.2003.09.015

Experimental method

X-RAY DIFFRACTION (2 Å)