1FAT

PHYTOHEMAGGLUTININ-L

1FAT の概要

• エントリーDOI: 10.2210/pdb1fat/pdb
• 分子名称: PHYTOHEMAGGLUTININ-L, 2-acetamido-2-deoxy-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: glycoprotein, plant defense protein, lectin
• 由来する生物種: Phaseolus vulgaris
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 111017.94

構造登録者

Hamelryck, T.,Loris, R. (登録日: 1996-06-12, 公開日: 1996-12-23, 最終更新日: 2024-10-23)

主引用文献

Hamelryck, T.W.,Dao-Thi, M.H.,Poortmans, F.,Chrispeels, M.J.,Wyns, L.,Loris, R.
The crystallographic structure of phytohemagglutinin-L.
J.Biol.Chem., 271:20479-20485, 1996

PubMed Abstract: The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed lectin from Phaseolus vulgaris, has been solved with molecular replacement using the coordinates of lentil lectin as model, and refined at a resolution of 2.8 A. The final R-factor of the structure is 20.0%. The quaternary structure of the PHA-L tetramer differs from the structures of the concanavalin A and peanut lectin tetramers, but resembles the structure of the soybean agglutinin tetramer. PHA-L consists of two canonical legume lectin dimers that pack together through the formation of a close contact between two beta-strands. Of the two covalently bound oligosaccharides per monomer, only one GlcNAc residue per monomer is visible in the electron density. In this article we describe the structure of PHA-L, and we discuss the putative position of the high affinity adenine-binding site present in a number of legume lectins. A comparison with transthyretin, a protein that shows a remarkable resemblance to PHA-L, gives further ground to our proposal.

PubMed: 8702788
DOI: 10.1074/jbc.271.34.20479

実験手法

X-RAY DIFFRACTION (2.8 Å)