CRYSTAL-STRUCTURE OF MOMORDIN, A TYPE-I RIBOSOME-INACTIVATING PROTEIN FROM THE SEEDS OF MOMORDICA-CHARANTIA

被引：56

作者：

HUSAIN, J

TICKLE, IJ

WOOD, SP

机构：

[1] Department of Crystallography, Birkbeck College, London, WC1E 7HX, Malet Street

来源：

FEBS LETTERS | 1994年 / 342卷 / 02期

关键词：

N-GLYCOSIDASE; ENZYME; RIBOSOME-INACTIVATING PROTEIN; RICIN; TRICHOSANTHIN; POKEWEED ANTIVIRAL PROTEIN;

D O I：

10.1016/0014-5793(94)80491-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A type I ribosome-inactivating protein, extracted and purified from M. charantia seeds, was crystallised by vapour diffusion with polyethylene glycol at pH 7.2. X-ray data were collected to 2.1 Angstrom resolution and the structure solved by molecular replacement using the A-chain coordinates of ricin. The overall fold of the protein is similar to ricin but there are differences in secondary structure, on the surface and in the active site cleft. These differences are probably due in part to the evolution of the protein without a B-chain partner. The most extensive reorganisation occurs at the C-terminus whereas Tyr(70) shows the greatest change in the active site cleft.

引用

页码：154 / 158

页数：5

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