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X-ray structure of an anti-fungal chitosanase from streptomyces N174

Nature Structural Biology volume 3, pages 155–162 (1996)Cite this article

Abstract

We report the 2.4 Å X-ray crystal structure of a protein with chitosan endo-hydrolase activity isolated from Streptomyces N174. The structure was solved using phases acquired by SIRAS from a two-site methyl mercury derivative combined with solvent flattening and non-crystallographic two-fold symmetry averaging, and refined to an R-factor of 18.5%. The mostly α-helical fold reveals a structural core shared with several classes of lysozyme and barley endochitinase, in spite of a lack of shared sequence. Based on this structural similarity we postulate a putative active site, mechanism of action and mode of substrate recognition. It appears that Glu 22 acts as an acid and Asp 40 serves as a general base to activate a water molecule for an SN2 attack on the glycosidic bond. A series of amino-acid side chains and backbone carbonyl groups may bind the polycationic chitosan substrate in a deep electronegative binding cleft.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry University of Texas Austin, Texas, 78712, USA

    Edward M. Marcotte, Arthur F. Monzingo, Stephen R. Ernst & Jon D. Robertas

  2. Groupe de Recherche en Biologie des Actinomyctes Departement de Biologie, Faculte des Sciences, Universite de Sherbrooke, Sherbrooke, Qubec, J1K 2R1, Canada

    Ryszard Brzezinski

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Marcotte, E., Monzingo, A., Ernst, S. et al. X-ray structure of an anti-fungal chitosanase from streptomyces N174. Nat Struct Mol Biol 3, 155–162 (1996). https://doi.org/10.1038/nsb0296-155

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