Crystallization and preliminary X-ray analysis of recombinant Glomerella cingulata cutinase

Cutinase catalyzes the hydrolysis of water‐soluble esters and long‐chain triglycerides and belongs to the family of serine hydrolases. The enzyme is thought to represent an evolutionary link between the esterase and lipase families and has potential applications in a wide range of industrial hydroly...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2008-06, Vol.64 (6), p.504-508
Main Authors: Nyon, Mun Peak, Rice, David W., Berrisford, John M., Huang, Huazhang, Moir, Arthur J. G., Craven, C. Jeremy, Nathan, Sheila, Mahadi, Nor Muhammad, Abu Bakar, Farah Diba
Format: Article
Language:English
Subjects:
Binding Sites
Carboxylic Ester Hydrolases - chemistry
Carboxylic Ester Hydrolases - genetics
Carboxylic Ester Hydrolases - isolation & purification
Crystallization
Crystallization Communications
cutinase
Escherichia coli - genetics
Glomerella cingulata
Glycine - chemistry
inhibitor complexes
Phyllachorales - enzymology
Protein Binding
Protein Folding
Protein Structure, Secondary
Recombinant Proteins - chemistry
Serine - chemistry
X-Ray Diffraction
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Summary:Cutinase catalyzes the hydrolysis of water‐soluble esters and long‐chain triglycerides and belongs to the family of serine hydrolases. The enzyme is thought to represent an evolutionary link between the esterase and lipase families and has potential applications in a wide range of industrial hydrolytic processes, for which an understanding of the molecular basis of its substrate specificity is critical. Glomerella cingulata cutinase has been cloned and the protein has been overexpressed in Escherichia coli, purified and subsequently crystallized in a wide range of different crystal forms in the presence and absence of inhibitors. The best crystals are those of the apo cutinase, which diffract to beyond 1.6 Å resolution and belong to space group P41212 or P43212. Crystals of cutinase with the inhibitors PETFP or E600 belong to space groups P212121 and P21, respectively, and diffract to approximately 2.5 Å resolution. All of the crystals are suitable for structural studies, which are currently ongoing.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309108012086