6FX3

crystal structure of Pholiota squarrosa lectin in complex with a dodecasaccharide

6FX3 の概要

• エントリーDOI: 10.2210/pdb6fx3/pdb
• 分子名称: lectin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]1-azido-beta-N-acetyl-D-glucosamine, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]1-azido-beta-N-acetyl-D-glucosamine, ... (4 entities in total)
• 機能のキーワード: lectin, dodecasaccharide, sugar binding protein
• 由来する生物種: Pholiota squarrosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12940.72

構造登録者

Cabanettes, A.,Varrot, A. (登録日: 2018-03-08, 公開日: 2018-07-11, 最終更新日: 2024-11-20)

主引用文献

Cabanettes, A.,Perkams, L.,Spies, C.,Unverzagt, C.,Varrot, A.
Recognition of Complex Core-Fucosylated N-Glycans by a Mini Lectin.
Angew. Chem. Int. Ed. Engl., 57:10178-10181, 2018

PubMed Abstract: The mini fungal lectin PhoSL was recombinantly produced and characterized. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with α1,6-linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, the crystal structure was solved using the zinc anomalous signal, and revealed an interlaced trimer creating a novel protein fold termed β-prism III. Three biantennary core-fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of α1,6-fucosylated N-glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse into N-glycan flexibility upon binding.

PubMed: 29956878
DOI: 10.1002/anie.201805165

実験手法

X-RAY DIFFRACTION (1.7 Å)