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CRYSTALLOGRAPHIC STUDY OF A RECOMBINANT CUTINASE FROM FUSARIUM SOLANIPISI
Martinez, Chrislaine Abergel, Chantal Cambillau, Christian de Geus, Pieter Lauwereys, Mark
Martinez, Chrislaine
Abergel, Chantal
Cambillau, Christian
de Geus, Pieter
Lauwereys, Mark
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Issue Date
1991
Submitted date
2024-03-13
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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.
Citation
Lipases : structure, mechanism and genetic engineering, 67 - 70
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International