A structural study of Hypocrea jecorina Cel5A

Interest in generating lignocellulosic biofuels through enzymatic hydrolysis continues to rise as nonrenewable fossil fuels are depleted. The high cost of producing cellulases, hydrolytic enzymes that cleave cellulose into fermentable sugars, currently hinders economically viable biofuel production....

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Veröffentlicht in:Protein science 2011-11, Vol.20 (11), p.1935-1940
Hauptverfasser: Lee, Toni M., Farrow, Mary F., Arnold, Frances H., Mayo, Stephen L.
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container_issue 11
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container_title Protein science
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creator Lee, Toni M.
Farrow, Mary F.
Arnold, Frances H.
Mayo, Stephen L.
description Interest in generating lignocellulosic biofuels through enzymatic hydrolysis continues to rise as nonrenewable fossil fuels are depleted. The high cost of producing cellulases, hydrolytic enzymes that cleave cellulose into fermentable sugars, currently hinders economically viable biofuel production. Here, we report the crystal structure of a prevalent endoglucanase in the biofuels industry, Cel5A from the filamentous fungus Hypocrea jecorina. The structure reveals a general fold resembling that of the closest homolog with a high‐resolution structure, Cel5A from Thermoascus aurantiacus. Consistent with previously described endoglucanase structures, the H. jecorina Cel5A active site contains a primarily hydrophobic substrate binding groove and a series of hydrogen bond networks surrounding two catalytic glutamates. The reported structure, however, demonstrates stark differences between side‐chain identity, loop regions, and the number of disulfides. Such structural information may aid efforts to improve the stability of this protein for industrial use while maintaining enzymatic activity through revealing nonessential and immutable regions. PDB Code(s): 3QR3
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The high cost of producing cellulases, hydrolytic enzymes that cleave cellulose into fermentable sugars, currently hinders economically viable biofuel production. Here, we report the crystal structure of a prevalent endoglucanase in the biofuels industry, Cel5A from the filamentous fungus Hypocrea jecorina. The structure reveals a general fold resembling that of the closest homolog with a high‐resolution structure, Cel5A from Thermoascus aurantiacus. Consistent with previously described endoglucanase structures, the H. jecorina Cel5A active site contains a primarily hydrophobic substrate binding groove and a series of hydrogen bond networks surrounding two catalytic glutamates. The reported structure, however, demonstrates stark differences between side‐chain identity, loop regions, and the number of disulfides. Such structural information may aid efforts to improve the stability of this protein for industrial use while maintaining enzymatic activity through revealing nonessential and immutable regions. 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subjects Amino Acid Sequence
Biodiesel fuels
biofuel
Biofuels
Catalytic Domain
Cel5A
cellulase
Cellulase - chemistry
cellulose
Chemical Phenomena
Crystal structure
Crystallization
Disulfides - chemistry
endoglucanase
Hydrogen Bonding
Hypocrea - enzymology
Hypocrea jecorina
Models, Molecular
Protein Binding
Protein Conformation
Protein Structure Report
Sequence Homology, Amino Acid
Thermoascus aurantiacus
title A structural study of Hypocrea jecorina Cel5A
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