5WEY

Joint X-ray/neutron structure of Concanavalin A with alpha1-2 D-mannobiose

5WEY の概要

• エントリーDOI: 10.2210/pdb5wey/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900111
• 分子名称: Concanavalin-A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: lectin, carbohydrate complex, protonation state, hydrogen bonding, neutron crystallography, sugar binding protein
• 由来する生物種: Canavalia ensiformis (Jack bean); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26059.70

構造登録者

Kovalevsky, A.,Gerlits, O.O.,Woods, R.J. (登録日: 2017-07-11, 公開日: 2017-09-13, 最終更新日: 2023-10-04)

主引用文献

Gerlits, O.O.,Coates, L.,Woods, R.J.,Kovalevsky, A.
Mannobiose Binding Induces Changes in Hydrogen Bonding and Protonation States of Acidic Residues in Concanavalin A As Revealed by Neutron Crystallography.
Biochemistry, 56:4747-4750, 2017

PubMed Abstract: Plant lectins are carbohydrate-binding proteins with various biomedical applications. Concanavalin A (Con A) holds promise in treating cancerous tumors. To better understand the Con A carbohydrate binding specificity, we obtained a room-temperature neutron structure of this legume lectin in complex with a disaccharide Manα1-2Man, mannobiose. The neutron structure afforded direct visualization of the hydrogen bonding between the protein and ligand, showing that the ligand is able to alter both protonation states and interactions for residues located close to and distant from the binding site. An unprecedented low-barrier hydrogen bond was observed forming between the carboxylic side chains of Asp28 and Glu8, with the D atom positioned equidistant from the oxygen atoms having an O···D···O angle of 101.5°.

PubMed: 28846383
DOI: 10.1021/acs.biochem.7b00654

実験手法

NEUTRON DIFFRACTION (2.5 Å)
X-RAY DIFFRACTION (1.8 Å)