1WW7

Agrocybe cylindracea galectin (Ligand-free)

1WW7 の概要

• エントリーDOI: 10.2210/pdb1ww7/pdb
• 関連するPDBエントリー: 1WW4 1WW5 1WW6
• 分子名称: galectin, SULFATE ION (3 entities in total)
• 機能のキーワード: agrocybe cylindracea galectin, fungal galectin, carbohydrate recognition domain, x-ray crystallographic analysis, sulfate ion, sugar binding protein
• 由来する生物種: Agrocybe cylindracea
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 68019.23

構造登録者

Ban, M.,Yoon, H.J.,Demirkan, E.,Utsumi, S.,Mikami, B.,Yagi, F. (登録日: 2005-01-03, 公開日: 2005-08-23, 最終更新日: 2024-03-13)

主引用文献

Ban, M.,Yoon, H.J.,Demirkan, E.,Utsumi, S.,Mikami, B.,Yagi, F.
Structural Basis of a Fungal Galectin from Agrocybe cylindracea for Recognizing Sialoconjugate
J.Mol.Biol., 351:695-706, 2005

PubMed Abstract: Galectin from an edible fungus Agrocybe cylindracea (ACG) has a strong preference for N-acetylneuraminyl lactose (NeuAcalpha2-3lactose). The sugar recognition mechanism of ACG was explored by the X-ray crystallographic analyses of ligand-free ACG, and its complex with lactose, 3'-sulfonyl lactose and NeuAcalpha2-3lactose. The refined structure shows that ACG is a "proto"-type galectin composed of a beta-sandwich of two antiparallel sheets, each with six strands, in contrast to the five and six strands in animal galectins. ACG dimer in solution was classified as being among the "layer"-type. The carbohydrate recognition domain (CRD) of this galectin is common to those of animal galectins, except for substitution of one residue, Ala64, which corresponds to Asn46 in human galectin 1. A five-residue insertion in ACG at positions 42-46 involving Ser44 and Asn46 modified the architecture of the sugar binding site that contributes sialic acid specificity. Furthermore, it was found that the binding of a sulfate ion near the CRD in the ligand-free form led to a change in the conformation of the loop region caused by main-chain cis/trans transition between Ser44 and Pro45.

PubMed: 16051274
DOI: 10.1016/j.jmb.2005.06.045

実験手法

X-RAY DIFFRACTION (1.9 Å)