Crystallization and preliminary crystallographic studies of AAL‐2, a novel lectin from Agrocybe aegerita that binds nonreducing terminal N‐acetylglucosamine. Issue 6 (31st May 2013)

• Record Type: Journal Article
• Authors: Ren, Xiaoming; Jiang, Shuai; Li, Defeng; Sun, Hui; Wang, Dacheng
• Is Part Of: Acta crystallographica. Volume 69:Issue 6(2013:Jun.)
• Page Start: 650
• Page End: 652
• Publication Date: 2013-05-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113011639
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>AAL‐2 is a recently discovered lectin from the mushroom <italic>Agrocybe aegerita</italic> that specifically recognizes nonreducing terminal acetylglucosamine (GlcNAc) and that could be used as a probe in studies of protein O‐linked β‐<italic>N</italic>‐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 <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 52.60, <italic>b</italic> = 111.70, <italic>c</italic> = 135.97 Å.</p> </abstract>