2QKD

Crystal structure of tandem ZPR1 domains

Summary for 2QKD

• Entry DOI: 10.2210/pdb2qkd/pdb
• Descriptor: Zinc finger protein ZPR1, ZINC ION, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: helical hairpins, beta helix, anti-parrallel beta sheet, double straded anti-parallel beta helix, metal binding protein, signaling protein, cell cycle
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: Q62384
• Total number of polymer chains: 1
• Total formula weight: 45631.80

Authors

Mishra, A.K. (deposition date: 2007-07-10, release date: 2007-08-07, Last modification date: 2024-04-03)

Primary citation

Mishra, A.K.,Gangwani, L.,Davis, R.J.,Lambright, D.G.
Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes.
Proc.Natl.Acad.Sci.Usa, 104:13930-13935, 2007

PubMed Abstract: Eukaryotic genomes encode a zinc finger protein (ZPR1) with tandem ZPR1 domains. In response to growth stimuli, ZPR1 assembles into complexes with eukaryotic translation elongation factor 1A (eEF1A) and the survival motor neurons protein. To gain insight into the structural mechanisms underlying the essential function of ZPR1 in diverse organisms, we determined the crystal structure of a ZPR1 domain tandem and characterized the interaction with eEF1A. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. However, ZPR1 efficiently displaces the exchange factor eEF1Balpha from preformed nucleotide-free complexes, suggesting that it may function as a negative regulator of eEF1A activation. Structure-based mutational and complementation analyses reveal a conserved binding epitope for eEF1A that is required for normal cell growth, proliferation, and cell cycle progression. Structural differences between the ZPR1 domains contribute to the observed functional divergence and provide evidence for distinct modalities of interaction with eEF1A and survival motor neuron complexes.

PubMed: 17704259
DOI: 10.1073/pnas.0704915104

Experimental method

X-RAY DIFFRACTION (2 Å)