Insights into interfacial activation from an open structure of Candida rugosa lipase.

摘要: The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with solvent-accessible active site. Comparison crystal homologous from Geotrichum candidum, in which site is covered by surface loops and inaccessible solvent, shows that largest structural differences occur vicinity Three this region differ significantly conformation, interfacial activation these lipases likely to be associated conformational rearrangements loops. "open" provides new image substrate binding access, different inferred "closed" form G. candidum lipase.