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J Biol Chem, Vol. 273, Issue 21, 12914-12922, May 22, 1998

Crystal Structure of the Arcelin-1 Dimer from Phaseolus vulgaris at 1.9-Å Resolution

Lionel Mourey, Jean-Denis Pédelacq, Catherine Birck, Christine Fabre^§, Pierre Rougé^§, and Jean-Pierre Samama

From the  Groupe de Cristallographie Biologique, and the ^§ Groupe Lectines et Reconnaissance, Institut de Pharmacologie et de Biologie Structurale, UPR 9062 CNRS, 205 route de Narbonne, F-31077 Toulouse CEDEX, France

Arcelin-1 is a glycoprotein from kidney beans (Phaseolus vulgaris) which displays insecticidal properties and protects the seeds from predation by larvae of various bruchids. This lectin-like protein is devoid of monosaccharide binding properties and belongs to the phytohemagglutinin protein family. The x-ray structure determination at 1.9-Å resolution of native arcelin-1 dimers, which correspond to the functional state of the protein in solution, was solved using multiple isomorphous replacement and refined to a crystallographic R factor of 0.208. The three glycosylation sites on each monomer are all covalently modified. One of these oligosaccharide chains provides interactions with protein atoms at the dimer interface, and another one may act by preventing the formation of higher oligomeric species in the arcelin variants. The dimeric structure and the severe alteration of the monosaccharide binding site in arcelin-1 correlate with the hemagglutinating properties of the protein, which are unaffected by simple sugars and sugar derivatives. Sequence analysis and structure comparisons of arcelin-1 with the other insecticidal proteins from kidney beans, arcelin-5, and -amylase inhibitor and with legume lectins, yield insights into the molecular basis of the different biological functions of these proteins.

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