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Glycosylated linkers in multi-modular lignocellulose degrading enzymes dynamically bind to cellulose

Christina M Payne, Michael G Resh, Liqun Chen, Michael F Crowley, Michael E Himmel, Larry E Taylor, Mats Sandgren, Jerry Ståhlberg, Ingeborg Stals (UGent) , Zhongping Tan, et al.
(2013) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 110(36). p.14646-14651
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Abstract
Plant cell wall polysaccharides represent a vast source of food in Nature. To depolymerize polysaccharides to soluble sugars, many organisms employ multi-functional enzyme cocktails 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 multi-modular with carbohydrate-binding modules (CBMs) and catalytic domains (CDs) 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 (Cel6A and Cel7A, 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.
Keywords
Biofuels, REESEI CELLOBIOHYDROLASE-I, carbohydrate recognition, post-translational modification, cellulase, glycosylation, MODULES, DEGRADATION, X-RAY, DISORDERED PROTEIN, MOLECULAR-DYNAMICS, SERRATIA-MARCESCENS, BIOMASS RECALCITRANCE, TRICHODERMA-REESEI, CRYSTALLINE CELLULOSE

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MLA
Payne, Christina M., et al. “Glycosylated Linkers in Multi-Modular Lignocellulose Degrading Enzymes Dynamically Bind to Cellulose.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 110, no. 36, 2013, pp. 14646–51, doi:10.1073/pnas.1309106110.
APA
Payne, C. M., Resh, M. G., Chen, L., Crowley, M. F., Himmel, M. E., Taylor, L. E., … Beckham, G. T. (2013). Glycosylated linkers in multi-modular lignocellulose degrading enzymes dynamically bind to cellulose. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(36), 14646–14651. https://doi.org/10.1073/pnas.1309106110
Chicago author-date
Payne, Christina M, Michael G Resh, Liqun Chen, Michael F Crowley, Michael E Himmel, Larry E Taylor, Mats Sandgren, et al. 2013. “Glycosylated Linkers in Multi-Modular Lignocellulose Degrading Enzymes Dynamically Bind to Cellulose.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 110 (36): 14646–51. https://doi.org/10.1073/pnas.1309106110.
Chicago author-date (all authors)
Payne, Christina M, Michael G Resh, Liqun Chen, Michael F Crowley, Michael E Himmel, Larry E Taylor, Mats Sandgren, Jerry Ståhlberg, Ingeborg Stals, Zhongping Tan, and Gregg T Beckham. 2013. “Glycosylated Linkers in Multi-Modular Lignocellulose Degrading Enzymes Dynamically Bind to Cellulose.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 110 (36): 14646–14651. doi:10.1073/pnas.1309106110.
Vancouver
1.
Payne CM, Resh MG, Chen L, Crowley MF, Himmel ME, Taylor LE, et al. Glycosylated linkers in multi-modular lignocellulose degrading enzymes dynamically bind to cellulose. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2013;110(36):14646–51.
IEEE
[1]
C. M. Payne et al., “Glycosylated linkers in multi-modular lignocellulose degrading enzymes dynamically bind to cellulose,” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 110, no. 36, pp. 14646–14651, 2013.
@article{3258201,
  abstract     = {{Plant cell wall polysaccharides represent a vast source of food in Nature. To depolymerize polysaccharides to soluble sugars, many organisms employ multi-functional enzyme cocktails 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 multi-modular with carbohydrate-binding modules (CBMs) and catalytic domains (CDs) 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 (Cel6A and Cel7A, 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.}},
  author       = {{Payne, Christina M and Resh, Michael G and Chen, Liqun and Crowley, Michael F and Himmel, Michael E and Taylor, Larry E and Sandgren, Mats and Ståhlberg, Jerry and Stals, Ingeborg and Tan, Zhongping and Beckham, Gregg T}},
  issn         = {{1091-6490}},
  journal      = {{PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}},
  keywords     = {{Biofuels,REESEI CELLOBIOHYDROLASE-I,carbohydrate recognition,post-translational modification,cellulase,glycosylation,MODULES,DEGRADATION,X-RAY,DISORDERED PROTEIN,MOLECULAR-DYNAMICS,SERRATIA-MARCESCENS,BIOMASS RECALCITRANCE,TRICHODERMA-REESEI,CRYSTALLINE CELLULOSE}},
  language     = {{eng}},
  number       = {{36}},
  pages        = {{14646--14651}},
  title        = {{Glycosylated linkers in multi-modular lignocellulose degrading enzymes dynamically bind to cellulose}},
  url          = {{http://doi.org/10.1073/pnas.1309106110}},
  volume       = {{110}},
  year         = {{2013}},
}
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