Crystallization and preliminary crystallographic studies of AAL-2, a novel lectin from Agrocybe aegerita that binds nonreducing terminal N-acetylglucosamine

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):650-2. doi: 10.1107/S1744309113011639. Epub 2013 May 24.

Abstract

AAL-2 is a recently discovered lectin from the mushroom Agrocybe aegerita that specifically recognizes nonreducing terminal acetylglucosamine (GlcNAc) and that could be used as a probe in studies of protein O-linked β-N-acetylglucosamination (O-GlyNAcylation). In order to illustrate the mechanism of how this protein specifically recognizes nonreducing terminal GlcNAc and to evaluate the efficacy of AAL-2 as a macromolecular probe in O-GlyNAcylation studies, expression and crystallization studies of AAL-2 were performed and a diffraction data set was collected to 2.0 Å resolution. Preliminary crystallographic studies revealed that the AAL-2 crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.60, b = 111.70, c = 135.97 Å.

Keywords: AAL-2; O-GlcNAcylation; lectin; nonreducing terminal N-acetylglucosamine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / chemistry*
  • Acetylglucosamine / metabolism*
  • Agrocybe*
  • Crystallization
  • Crystallography, X-Ray
  • Lectins / chemistry*
  • Lectins / metabolism*
  • Protein Binding / physiology

Substances

  • Lectins
  • Acetylglucosamine