Structure of the kinase domain of Gilgamesh from Drosophila melanogaster

Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):438-43. doi: 10.1107/S2053230X14004774. Epub 2014 Mar 25.

Abstract

The CK1 family kinases regulate multiple cellular aspects and play important roles in Wnt/Wingless and Hedgehog signalling. The kinase domain of Drosophila Gilgamesh isoform I (Gilgamesh-I), a homologue of human CK1-γ, was purified and crystallized. Crystals of methylated Gilgamesh-I kinase domain with a D210A mutation diffracted to 2.85 Å resolution and belonged to space group P43212, with unit-cell parameters a = b = 52.025, c = 291.727 Å. The structure of Gilgamesh-I kinase domain, which was determined by molecular replacement, has conserved catalytic elements and an active conformation. Structural comparison indicates that an extended loop between the α1 helix and the β4 strand exists in the Gilgamesh-I kinase domain. This extended loop may regulate the activity and function of Gilgamesh-I.

Keywords: CK1 family kinases; Drosophila melanogaster; Gilgamesh; kinase domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Casein Kinase I / chemistry*
  • Casein Kinase I / genetics
  • Casein Kinase I / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation / genetics
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Drosophila Proteins
  • Casein Kinase I
  • gish protein, Drosophila

Associated data

  • PDB/4NT4