Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Ruth MikeskaChristian Betzel

Abstract

The structures of mistletoe lectin I (ML-I) from Viscum album complexed with lactose and galactose have been determined at 2.3 A resolution and refined to R factors of 20.9% (Rfree = 23.6%) and 20.9 (Rfree = 24.6%), respectively. ML-I is a heterodimer and belongs to the class of ribosome-inactivating proteins of type II, which consist of two chains. The A-chain has rRNA N-glycosidase activity and irreversibly inhibits eukaryotic ribosomes. The B-chain is a lectin and preferentially binds to galactose-terminated glycolipids and glycoproteins on cell membranes. Saccharide binding is performed by two binding sites in subdomains alpha1 and gamma2 of the ML-I B-chain separated by approximately 62 A from each other. The favoured binding of galactose in subdomain alpha1 is achieved via hydrogen bonds connecting the 4-hydroxyl and 3-hydroxyl groups of the sugar moiety with the side chains of Asp23B, Gln36B and Lys41B and the main chain of 26B. The aromatic ring of Trp38B on top of the preferred binding pocket supports van der Waals packing of the apolar face of galactose and stabilizes the sugar-lectin complex. In the galactose-binding site II of subdomain gamma2, Tyr249B provides the hydrophobic stacking and the side chains of Asp235B...Continue Reading

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Citations

Aug 23, 2008·Biochimica Et Biophysica Acta·Arne MeyerChristian Betzel
Oct 17, 2007·Biochemical and Biophysical Research Communications·A MeyerCh Betzel
Jul 31, 2013·Acta Crystallographica. Section D, Biological Crystallography·Alok SharmaM Vijayan
Jul 1, 2010·Organic & Biomolecular Chemistry·Timo LeermannHans-Josef Altenbach
Aug 8, 2021·International Journal of Molecular Sciences·Soran Mohammed, Natalie Ferry

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