期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 369, 期 3, 页码 710-721出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.03.016
关键词
carbohydrate recognition; fungal lectin; mushroom agglutinin; protein-carbohydrate interactions; X-ray crystal structure
资金
- NIGMS NIH HHS [GM-29470] Funding Source: Medline
MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Gal alpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 angstrom resolution, in complex with the linear trisaccharide Gal alpha-(1,3) Gal beta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties. (c) 2007 Elsevier Ltd. All rights reserved.
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