4TQK

Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection

Summary for 4TQK

• Entry DOI: 10.2210/pdb4tqk/pdb
• Related: 4TQJ 4TQM
• Descriptor: Lectin 2, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: complex, lectin, glcnac, sugar binding protein
• Biological source: Agrocybe aegerita (Black poplar mushroom)
• Total number of polymer chains: 2
• Total formula weight: 88597.87

Authors

Hu, Y.L.,Ren, X.M.,Li, D.F.,Jiang, S.,Lan, X.Q.,Sun, H.,Wang, D.C. (deposition date: 2014-06-11, release date: 2015-06-03, Last modification date: 2024-03-20)

Primary citation

Ren, X.M.,Li, D.F.,Jiang, S.,Lan, X.Q.,Hu, Y.,Sun, H.,Wang, D.C.
Structural Basis of Specific Recognition of Non-Reducing Terminal N-Acetylglucosamine by an Agrocybe aegerita Lectin.
Plos One, 10:e0129608-e0129608, 2015

PubMed Abstract: O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a reversible post-translational modification that plays essential roles in many cellular pathways. Research in this field, however, is hampered by the lack of suitable probes to identify, accumulate, and purify the O-GlcNAcylated proteins. We have previously reported the identification of a lectin from the mushroom Agrocybe aegerita, i.e., Agrocybe aegerita lectin 2, or AAL2, that could bind terminal N-acetylglucosamine with higher affinities and specificity than other currently used probes. In this paper, we report the crystal structures of AAL2 and its complexes with GlcNAc and GlcNAcβ1-3Galβ1-4GlcNAc and reveal the structural basis of GlcNAc recognition by AAL2 and residues essential for the binding of terminal N-acetylglucosamine. Study on AAL2 may enable us to design a protein probe that can be used to identify and purify O-GlcNAcylated proteins more efficiently.

PubMed: 26114302
DOI: 10.1371/journal.pone.0129608

Experimental method

X-RAY DIFFRACTION (2.1 Å)