4MON

ORTHORHOMBIC MONELLIN

4MON の概要

• エントリーDOI: 10.2210/pdb4mon/pdb
• 分子名称: MONELLIN (3 entities in total)
• 機能のキーワード: sweet-tasting protein, orthorhombic crystals
• 由来する生物種: Dioscoreophyllum cumminsii (serendipity berry); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 22497.63

構造登録者

Bujacz, G.,Wlodawer, A. (登録日: 1997-03-04, 公開日: 1997-07-07, 最終更新日: 2024-05-22)

主引用文献

Bujacz, G.,Miller, M.,Harrison, R.,Thanki, N.,Gilliland, G.L.,Ogata, C.M.,Kim, S.H.,Wlodawer, A.
Structure of monellin refined to 2.3 a resolution in the orthorhombic crystal form.
Acta Crystallogr.,Sect.D, 53:713-719, 1997

PubMed Abstract: The structure of orthorhombic crystals of monellin, a sweet protein extracted from African serendipity berries, has been solved by molecular replacement and refined to 2.3 A resolution. The final R factor was 0.150 for a model with excellent geometry. A monellin molecule consists of two peptides that are non-covalently bound, with chain A composed of three beta-strands interconnected by loop regions and chain B composed of two beta-strands interconnected by an alpha-helix. The N terminus of chain A is in close proximity to the C terminus of chain B. The two molecules in the asymmetric unit are related by a non-crystallographic twofold axis and form a dimer, similar to those previously observed in other crystal forms of both natural and single-chain monellin. The r.m.s, deviation between the Calpha atoms in the two independent molecules is 0.60 A, while the deviations from the individual molecules in the previously reported monoclinic crystals are 0.50-0.57 A. This result proves that the structure of monellin is not significantly influenced by crystal packing forces.

PubMed: 15299859
DOI: 10.1107/S0907444997006860

実験手法

X-RAY DIFFRACTION (2.3 Å)