Crystal structure of momordin, a type I Ribosome Inactivating Protein from the seeds of Momordica charantia

FEBS Letters

Wood, Stephen P.¹  Husain, Jasmine¹  Tickle, Ian J.¹ 

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

关键词: N-Glycosidase;    Enzyme;    Ribosome-inactivating protein;    Ricin;    Trichosanthin;    Pokeweed antiviral protein;    RIP;    ribosome-inactivating protein;    RTA;    ricin A-chain;    RTC;    recombinant ricin;    MOM;    momordin;    PAP;    pokeweed antiviral protein;    FMP;    formycin monophosphate;    ApG;    adenyl(3'-5')guanosine;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)80491-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 Å 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 Tyr⁷⁰ shows the greatest change in the active site cleft.

【 授权许可】

Unknown