Nature Structural Biology
1, 36 - 47 (1994)
doi:10.1038/nsb0194-36
An unusual buried polar cluster in a family of fungal lipasesU. Derewenda1, L. Swenson1, R. Green1, Y. Wei1, G.G. Dodson2, S. Yamaguchi3, M.J. Haas4
& Z.S. Derewenda1
1Medical Research Council of Canada Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7
2Department of Chemistry, University of York, Heslington, York, Y01 5DD U.K.
3Tsukuba Research Laboratories, Amano Pharmaceutical Co. Ltd., 22 Miyukigaoka, Tsukuba, Ibaraki 305, Japan
4US Dept. of Agriculture, Agricultural Research Service, North Atlantic Area Eastern Regional Research Center, 600 East Mermaid Lane, Philadelphia, PA 19118, USA The stability of globular proteins arises largely from the burial of non−polar amino acids in their interior. These residues are efficiently packed to eliminate energetically unfavorable cavities. Contrary to these observations, high resolution X−ray crystallographic analyses of four homologous lipases from filamentous fungi reveal an  / fold which contains a buried conserved constellation of charged and polar side chains with associated cavities containing ordered water molecules. It is possible that this structural arrangement plays an important role in interfacial catalysis.
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