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Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.

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Title: Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.
Authors: Payne, Christina M.1,2, Resch, Michael G.1, Liqun Chen3, Crowley, Michael F.1, Himmel, Michael E.1, Taylor II, Larry E.1, Sandgren, Mats4, Ståhlberg, Jerry4, Stals, Ingeborg5,6 ingeborg.stals@hogent.be, Zhongping Tan3 zhongping.tan@colorado.edu, Beckham, Gregg T.7,8 gregg.beckham@nrel.gov
Source: Proceedings of the National Academy of Sciences of the United States of America. 9/3/2013, Vol. 110 Issue 36, p14646-14651. 6p.
Subjects: Lignocellulose, Plant cell walls, Polysaccharides, Molecular dynamics, Enzyme activation
Abstract: Plant cell-wall polysaccharides represent a vast source of food in nature. To depolymerize polysaccharides to soluble sugars, many organisms use multifunctional enzyme mixtures consisting of glycoside hydrolases, lytic polysaccharide mono-oxygenases, polysaccharide lyases, and carbohydrate esterases, as well as accessory, redox-active enzymes for lignin depolymerization. Many of these enzymes that degrade lignocellulose are multimodular with carbohydrate-binding modules (CBMs) and catalytic domains connected by flexible, glycosylated linkers. These linkers have long been thought to simply serve as a tether between structured domains or to act in an inchworm-like fashion during catalytic action. To examine linker function, we performed molecular dynamics (MD) simulations of the Trichoderma reesei Family 6 and Family 7 cellobiohydrolases (TrCel6A and TrCel7A, respectively) bound to cellulose. During these simulations, the glycosylated linkers bind directly to cellulose, suggesting a previously unknown role in enzyme action. The prediction from the MD simulations was examined experimentally by measuring the binding affinity of the Cel7A CBM and the natively glycosylated Cel7A CBM-linker. On crystalline cellulose, the glycosylated linker enhances the binding affinity over the CBM alone by an order of magnitude. The MD simulations before and after binding of the linker also suggest that the bound linker may affect enzyme action due to significant damping in the enzyme fluctuations. Together, these results suggest that glycosylated linkers in carbohydrate-active enzymes, which are intrinsically disordered proteins in solution, aid in dynamic binding during the enzymatic deconstruction of plant cell walls. [ABSTRACT FROM AUTHOR]
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.
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  Data: <searchLink fieldCode="AR" term="%22Payne%2C+Christina+M%2E%22">Payne, Christina M.</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Resch%2C+Michael+G%2E%22">Resch, Michael G.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Liqun+Chen%22">Liqun Chen</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Crowley%2C+Michael+F%2E%22">Crowley, Michael F.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Himmel%2C+Michael+E%2E%22">Himmel, Michael E.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Taylor+II%2C+Larry+E%2E%22">Taylor II, Larry E.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Sandgren%2C+Mats%22">Sandgren, Mats</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Ståhlberg%2C+Jerry%22">Ståhlberg, Jerry</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22Stals%2C+Ingeborg%22">Stals, Ingeborg</searchLink><relatesTo>5,6</relatesTo><i> ingeborg.stals@hogent.be</i><br /><searchLink fieldCode="AR" term="%22Zhongping+Tan%22">Zhongping Tan</searchLink><relatesTo>3</relatesTo><i> zhongping.tan@colorado.edu</i><br /><searchLink fieldCode="AR" term="%22Beckham%2C+Gregg+T%2E%22">Beckham, Gregg T.</searchLink><relatesTo>7,8</relatesTo><i> gregg.beckham@nrel.gov</i>
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  Data: <searchLink fieldCode="DE" term="%22Lignocellulose%22">Lignocellulose</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+cell+walls%22">Plant cell walls</searchLink><br /><searchLink fieldCode="DE" term="%22Polysaccharides%22">Polysaccharides</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+activation%22">Enzyme activation</searchLink>
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  Data: Plant cell-wall polysaccharides represent a vast source of food in nature. To depolymerize polysaccharides to soluble sugars, many organisms use multifunctional enzyme mixtures consisting of glycoside hydrolases, lytic polysaccharide mono-oxygenases, polysaccharide lyases, and carbohydrate esterases, as well as accessory, redox-active enzymes for lignin depolymerization. Many of these enzymes that degrade lignocellulose are multimodular with carbohydrate-binding modules (CBMs) and catalytic domains connected by flexible, glycosylated linkers. These linkers have long been thought to simply serve as a tether between structured domains or to act in an inchworm-like fashion during catalytic action. To examine linker function, we performed molecular dynamics (MD) simulations of the Trichoderma reesei Family 6 and Family 7 cellobiohydrolases (TrCel6A and TrCel7A, respectively) bound to cellulose. During these simulations, the glycosylated linkers bind directly to cellulose, suggesting a previously unknown role in enzyme action. The prediction from the MD simulations was examined experimentally by measuring the binding affinity of the Cel7A CBM and the natively glycosylated Cel7A CBM-linker. On crystalline cellulose, the glycosylated linker enhances the binding affinity over the CBM alone by an order of magnitude. The MD simulations before and after binding of the linker also suggest that the bound linker may affect enzyme action due to significant damping in the enzyme fluctuations. Together, these results suggest that glycosylated linkers in carbohydrate-active enzymes, which are intrinsically disordered proteins in solution, aid in dynamic binding during the enzymatic deconstruction of plant cell walls. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1073/pnas.1309106110
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      – Code: eng
        Text: English
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        PageCount: 6
        StartPage: 14646
    Subjects:
      – SubjectFull: Lignocellulose
        Type: general
      – SubjectFull: Plant cell walls
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      – SubjectFull: Polysaccharides
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      – SubjectFull: Molecular dynamics
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      – SubjectFull: Enzyme activation
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      – TitleFull: Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose.
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              Text: 9/3/2013
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