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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 ?-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.

SUBMITTER: Ren X

PROVIDER: S-EPMC3668585 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature

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

Ren Xiaoming X Jiang Shuai S Li Defeng D Sun Hui H Wang Dacheng D

Acta crystallographica. Section F, Structural biology and crystallization communications 20130524 Pt 6

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 ...[more]

PMID: 23722844

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A novel lectin from Agrocybe aegerita shows high binding selectivity for terminal N-acetylglucosamine.

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