2CAU

CANAVALIN FROM JACK BEAN

2CAU の概要

• エントリーDOI: 10.2210/pdb2cau/pdb
• 分子名称: PROTEIN (CANAVALIN) (2 entities in total)
• 機能のキーワード: vicilin, 7s seed protein, domain duplication, swiss roll, plant protein
• 由来する生物種: Canavalia ensiformis (jack bean)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50383.47

構造登録者

Ko, T.-P.,Day, J.,Macpherson, A. (登録日: 1998-11-20, 公開日: 1998-11-25, 最終更新日: 2023-08-23)

主引用文献

Ko, T.P.,Day, J.,McPherson, A.
The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution.
Acta Crystallogr.,Sect.D, 56:411-420, 2000

PubMed Abstract: The structure of canavalin was refined to 2.1 and 2.0 A resolution in cubic and hexagonal crystals of space group P2(1)3 and P6(3), respectively. The threefold molecular symmetry is expressed in the symmetry of both crystals, where each identical subunit is an asymmetric unit. The canavalin subunit consists of two very similar domains, each comprised of a core subdomain having Swiss-roll topology with a loop subdomain that contains helices. The refined canavalin models resolved the discrepancy in amino-acid registers of the secondary-structural elements compared with phaseolin. The presence of strand Z in both domains of canavalin was confirmed and a new helix in the loop between strands A and B of each domain was observed. The models were analyzed in terms of the duplicated vicilin domains. Three strictly conserved residues, two glycines and a proline, were identified. The similarity between entire vicilin molecules is greater than that between separate domains of canavalin and phaseolin. Homology modeling of the sucrose-binding protein (SBP) from soybean showed a plausible trimeric assembly of subunits similar to that of vicilins.

PubMed: 10739914
DOI: 10.1107/S0907444900002237

実験手法

X-RAY DIFFRACTION (2.1 Å)