Crystallization and preliminary crystallographic studies of the W2 domain of Drosophila melanogaster eukaryotic translation initiation factor 5C domain-containing protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1315-7. doi: 10.1107/S1744309112036512. Epub 2012 Oct 30.

Abstract

The Drosophila melanogaster eukaryotic translation initiation factor 5C domain-containing protein (ECP) is composed of two independently folded domains which belong to the basic leucine-zipper and W2 domain-containing protein (BZW) family. Based on the sequence similarity between the C-terminal W2 domain of ECP and some eukaryotic translation initiation factors (such as eIF2Bℇ, eIF4γ, eIF5 etc.), ECP has been speculated to participate in the translation initiation process. Structural information on the C-terminal W2 domain of ECP would be helpful in understanding the specific cellular function of this protein. Here, the W2 domain of ECP was expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.70 Å resolution and belonged to space group I4, with unit-cell parameters a=b=81.05, c=57.44 Å. The Matthews coefficient suggested that there was one molecule per asymmetric unit in the crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Drosophila Proteins / chemistry*
  • Drosophila melanogaster / chemistry*
  • Eukaryotic Initiation Factor-5 / chemistry*
  • Protein Structure, Tertiary

Substances

  • Drosophila Proteins
  • Eukaryotic Initiation Factor-5