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Crystal structure of momordin, a type I Ribosome Inactivating Protein from the seeds of Momordica charantia
Author(s) -
Husain Jasmine,
Tickle Ian J.,
Wood Stephen P.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80491-5
Subject(s) - momordica , ribosome inactivating protein , ricin , chemistry , molecular replacement , ribosome , active site , protein secondary structure , biochemistry , crystallography , protein structure , enzyme , rna , medicine , gene , traditional medicine , toxin
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 Tyr 70 shows the greatest change in the active site cleft.