title: Crystallization and preliminary crystallographic studies of AAL-2, a novel lectin from Agrocybe aegerita that binds nonreducing terminal N-acetylglucosamine.
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.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Ren
authors.forename: Shuai
authors.initials: S
authors.lastname: Jiang
authors.forename: Defeng
authors.initials: D
authors.lastname: Li
authors.forename: Hui
authors.initials: H
authors.lastname: Sun
authors.forename: Dacheng
authors.initials: D
authors.lastname: Wang
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry* / Q000378:metabolism*; D055362:Agrocybe; D003460:Crystallization; D018360:Crystallography, X-Ray; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology
chemical_list: D037102:Lectins; D000117:Acetylglucosamine
keywords: AAL-2; O-GlcNAcylation; lectin; nonreducing terminal N-acetylglucosamine