Crystallization of the ribosome inactivating protein ML l from VISCUM ALBUM (mistletoe) complexed with ß-D-galactose

Journal/Book: J. Mol. Biol. 234, 1279-1281. 1993;

Abstract: A ribosome inactivating protein (ML1) from the mistletoe plant (Viscumalbum) has been crystallized. The crystals, grown in the presence ofbeta-D-galactose, are hexagonal, space group P6(1)22 or P6(5)22, a = b =111.0 A, c = 309.3 A with 24 molecules per unit cell (assuming 33%solvent by weight). The protein of molecular mass 63 kDa is aheterodimer consisting of two chains, A and B, joined by a disulfidebond. The A-chain, 29 kDa, inhibits protein synthesis by depurinating anadenine residue (A4324) in a highly conserved RNA loop of the 28 Sribosomal subunit. The toxicity of the protein is mediated by theB-chain, 34 kDa, which has lectin activity, interacting with sugarresidues of glycoproteins and glycolipids on the surface of targetcells. Author.

Keyword(s): CRYSTALLOGRAPHY-X-RAY

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