5J76

Structure of Lectin from Colocasia esculenta(L.) Schott

5J76 の概要

• エントリーDOI: 10.2210/pdb5j76/pdb
• 分子名称: 12kD storage protein, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: sugar binding, lectin, colocasia agglutinin, sugar binding protein
• 由来する生物種: Colocasia esculenta (Wild taro); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24578.28

構造登録者

Vajravijayan, S.,Pletnev, S.,Nandhagopal, N.,Gunasekaran, K. (登録日: 2016-04-06, 公開日: 2016-06-22, 最終更新日: 2024-11-06)

主引用文献

Vajravijayan, S.,Pletnev, S.,Pletnev, V.Z.,Nandhagopal, N.,Gunasekaran, K.
Structural analysis of beta-prism lectin from Colocasia esculenta (L.) S chott.
Int.J.Biol.Macromol., 91:518-523, 2016

PubMed Abstract: The Mannose-binding β-Prism Colocasia esculenta lectin (β-PCL) was purified from tubers using ion exchange chromatography. The purified β-PCL appeared as a single band of ∼12kDa on SDS-PAGE. β-PCL crystallizes in trigonal space group P3121 and diffracted to a resolution of 2.1Å. The structure was solved using Molecular replacement using Crocus vernus lectin (PDB: 3MEZ) as a model. From the final refined model to an R-factor of 16.5% and an Rfree of 20.4%, it has been observed that the biological unit consists of two β-Prism domains augmented through C-terminals swap over to form one of faces for each domain. Cα superposition of individual domains of β-PCL with individual domains of other related structures and superposition of whole protein structures were carried out. The higher RMS deviation for the superposition of whole structures suggest that β-prism domains assume different orientation in each structure.

PubMed: 27262515
DOI: 10.1016/j.ijbiomac.2016.05.048

実験手法

X-RAY DIFFRACTION (2.1 Å)