Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization

Xiongce Zhao; Tauna R. Rignall; Clare McCabe; William S. Adney; Michael E. Himmel

doi:10.1016/j.cplett.2008.05.060

Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization

Xiongce Zhao, Tauna R. Rignall, Clare McCabe^*, William S. Adney, Michael E. Himmel

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The calculations predict an energy storage mechanism of the linker under stretching/compression that is consistent with processive depolymerization. The linker exhibits two stable states at lengths of 2.5 nm and 5.5 nm during extension/compression, with a free energy difference of 10.5 kcal/mol between the two states separated by an energy barrier. The switching between stable states supports the hypothesis that the linker peptide has the capacity to store energy in a manner similar to a spring.

Original language	English
Pages (from-to)	284-288
Number of pages	5
Journal	Chemical Physics Letters
Volume	460
Issue number	1-3
DOIs	https://doi.org/10.1016/j.cplett.2008.05.060
Publication status	Published - 20 Jul 2008

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1016/j.cplett.2008.05.060

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title = "Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization",

abstract = "We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The calculations predict an energy storage mechanism of the linker under stretching/compression that is consistent with processive depolymerization. The linker exhibits two stable states at lengths of 2.5 nm and 5.5 nm during extension/compression, with a free energy difference of 10.5 kcal/mol between the two states separated by an energy barrier. The switching between stable states supports the hypothesis that the linker peptide has the capacity to store energy in a manner similar to a spring.",

author = "Xiongce Zhao and Rignall, {Tauna R.} and Clare McCabe and Adney, {William S.} and Himmel, {Michael E.}",

note = "Funding Information: The authors thank John Brady and Peter Cummings for helpful discussions. This work was supported by subcontract XCO-2-32-042-01 from the National Renewable Energy Laboratory funded by the U.S. DOE Office of the Biomass Program. The research was conducted at Vanderbilt University and the Center for Nanophase Materials Sciences, which is sponsored at Oak Ridge National Laboratory by the Division of Scientific User Facilities, U.S. Department of Energy. This research used resources of the National Energy Research Scientific Computing Center, which is supported by the Office of Science of the U.S. Department of Energy under Contract No. DE-AC02-05CH11231.",

year = "2008",

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doi = "10.1016/j.cplett.2008.05.060",

language = "English",

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T1 - Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization

AU - Zhao, Xiongce

AU - Rignall, Tauna R.

AU - McCabe, Clare

AU - Adney, William S.

AU - Himmel, Michael E.

N1 - Funding Information: The authors thank John Brady and Peter Cummings for helpful discussions. This work was supported by subcontract XCO-2-32-042-01 from the National Renewable Energy Laboratory funded by the U.S. DOE Office of the Biomass Program. The research was conducted at Vanderbilt University and the Center for Nanophase Materials Sciences, which is sponsored at Oak Ridge National Laboratory by the Division of Scientific User Facilities, U.S. Department of Energy. This research used resources of the National Energy Research Scientific Computing Center, which is supported by the Office of Science of the U.S. Department of Energy under Contract No. DE-AC02-05CH11231.

PY - 2008/7/20

Y1 - 2008/7/20

N2 - We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The calculations predict an energy storage mechanism of the linker under stretching/compression that is consistent with processive depolymerization. The linker exhibits two stable states at lengths of 2.5 nm and 5.5 nm during extension/compression, with a free energy difference of 10.5 kcal/mol between the two states separated by an energy barrier. The switching between stable states supports the hypothesis that the linker peptide has the capacity to store energy in a manner similar to a spring.

AB - We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The calculations predict an energy storage mechanism of the linker under stretching/compression that is consistent with processive depolymerization. The linker exhibits two stable states at lengths of 2.5 nm and 5.5 nm during extension/compression, with a free energy difference of 10.5 kcal/mol between the two states separated by an energy barrier. The switching between stable states supports the hypothesis that the linker peptide has the capacity to store energy in a manner similar to a spring.

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U2 - 10.1016/j.cplett.2008.05.060

DO - 10.1016/j.cplett.2008.05.060

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SN - 0009-2614

VL - 460

SP - 284

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JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1-3

ER -

Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization

Abstract

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