CRYSTALLOGRAPHIC STUDY OF A RECOMBINANT CUTINASE FROM FUSARIUM SOLANIPISI

Abstract

Cutinases are a group of extracellular fungal hydrolytic enzymes capable of degrading the insoluble lipid polyester matrix,i.e. cutin, which covers the surface of plants. Their weight is 22,000 Da, signifantly lower than all other lipases. A recombinant cutinase from F. solani pisi is expressed and excreted with very high yieldsin E. coli cultures. Cutinase wascrystallized (PEG 6000 15-20% ,pH 7.0 to 10.0,20°C) in space group P21 with cell dimensions 35.1A,67.4A,37.05 A, ß=94°.They diffract to 1.5 A resolution (Rsym=4.41%). Data from native and derivatives have been collected. MIR phasingis in progress.