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Amylose recognition and ring-size determination of amylomaltase

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Amylose recognition and ring-size determination of amylomaltase. / Roth, Christian; Weizenmann, Nicole; Bexten, Nicola; Saenger, Wolfram; Zimmermann, Wolfgang; Maier, Timm; Sträter, Norbert.

In: Science Advances, Vol. 3, No. 1, e1601386, 13.01.2017, p. 1-10.

Research output: Contribution to journalArticle

Harvard

Roth, C, Weizenmann, N, Bexten, N, Saenger, W, Zimmermann, W, Maier, T & Sträter, N 2017, 'Amylose recognition and ring-size determination of amylomaltase', Science Advances, vol. 3, no. 1, e1601386, pp. 1-10. https://doi.org/10.1126/sciadv.1601386

APA

Roth, C., Weizenmann, N., Bexten, N., Saenger, W., Zimmermann, W., Maier, T., & Sträter, N. (2017). Amylose recognition and ring-size determination of amylomaltase. Science Advances, 3(1), 1-10. [e1601386]. https://doi.org/10.1126/sciadv.1601386

Vancouver

Roth C, Weizenmann N, Bexten N, Saenger W, Zimmermann W, Maier T et al. Amylose recognition and ring-size determination of amylomaltase. Science Advances. 2017 Jan 13;3(1):1-10. e1601386. https://doi.org/10.1126/sciadv.1601386

Author

Roth, Christian ; Weizenmann, Nicole ; Bexten, Nicola ; Saenger, Wolfram ; Zimmermann, Wolfgang ; Maier, Timm ; Sträter, Norbert. / Amylose recognition and ring-size determination of amylomaltase. In: Science Advances. 2017 ; Vol. 3, No. 1. pp. 1-10.

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@article{5afb0cc996f949d295d07e92fa2cacfa,
title = "Amylose recognition and ring-size determination of amylomaltase",
abstract = "Starch is a major carbon and energy source throughout all kingdoms of life. It consists of two carbohydrate polymers, branched amylopectin and linear amylose, which are sparingly soluble in water. Hence, the enzymatic breakdown by glycoside hydrolases (GHs) is of great biological and societal importance. Amylomaltases (AMs) are GHs specialized in the hydrolysis of α-1,4-linked sugar chains such as amylose. They are able to catalyze an intramolecular transglycosylation of a bound sugar chain yielding polymeric sugar rings, the cycloamyloses (CAs), consisting of 20 to 100 glucose units. Despite a wealth of data on short oligosaccharide binding to GHs, no structural evidence is available for their interaction with polymeric substrates that better represent the natural polysaccharide. We have determined the crystal structure of Thermus aquaticus AM in complex with a 34-meric CA-one of the largest carbohydrates resolved by x-ray crystallography and a mimic of the natural polymeric amylose substrate. In total, 15 glucose residues interact with the protein in an extended crevice with a length of more than 40 {\AA}. A modified succinimide, derived from aspartate, mediates protein-sugar interactions, suggesting a biological role for this nonstandard amino acid. The structure, together with functional assays, provides unique insights into the interaction of GHs with their polymeric substrate and reveals a molecular ruler mechanism for minimal ring-size determination of CA products.",
author = "Christian Roth and Nicole Weizenmann and Nicola Bexten and Wolfram Saenger and Wolfgang Zimmermann and Timm Maier and Norbert Str{\"a}ter",
note = "2017 {\circledC} The Authors.",
year = "2017",
month = "1",
day = "13",
doi = "10.1126/sciadv.1601386",
language = "English",
volume = "3",
pages = "1--10",
journal = "Science Advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "1",

}

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TY - JOUR

T1 - Amylose recognition and ring-size determination of amylomaltase

AU - Roth, Christian

AU - Weizenmann, Nicole

AU - Bexten, Nicola

AU - Saenger, Wolfram

AU - Zimmermann, Wolfgang

AU - Maier, Timm

AU - Sträter, Norbert

N1 - 2017 © The Authors.

PY - 2017/1/13

Y1 - 2017/1/13

N2 - Starch is a major carbon and energy source throughout all kingdoms of life. It consists of two carbohydrate polymers, branched amylopectin and linear amylose, which are sparingly soluble in water. Hence, the enzymatic breakdown by glycoside hydrolases (GHs) is of great biological and societal importance. Amylomaltases (AMs) are GHs specialized in the hydrolysis of α-1,4-linked sugar chains such as amylose. They are able to catalyze an intramolecular transglycosylation of a bound sugar chain yielding polymeric sugar rings, the cycloamyloses (CAs), consisting of 20 to 100 glucose units. Despite a wealth of data on short oligosaccharide binding to GHs, no structural evidence is available for their interaction with polymeric substrates that better represent the natural polysaccharide. We have determined the crystal structure of Thermus aquaticus AM in complex with a 34-meric CA-one of the largest carbohydrates resolved by x-ray crystallography and a mimic of the natural polymeric amylose substrate. In total, 15 glucose residues interact with the protein in an extended crevice with a length of more than 40 Å. A modified succinimide, derived from aspartate, mediates protein-sugar interactions, suggesting a biological role for this nonstandard amino acid. The structure, together with functional assays, provides unique insights into the interaction of GHs with their polymeric substrate and reveals a molecular ruler mechanism for minimal ring-size determination of CA products.

AB - Starch is a major carbon and energy source throughout all kingdoms of life. It consists of two carbohydrate polymers, branched amylopectin and linear amylose, which are sparingly soluble in water. Hence, the enzymatic breakdown by glycoside hydrolases (GHs) is of great biological and societal importance. Amylomaltases (AMs) are GHs specialized in the hydrolysis of α-1,4-linked sugar chains such as amylose. They are able to catalyze an intramolecular transglycosylation of a bound sugar chain yielding polymeric sugar rings, the cycloamyloses (CAs), consisting of 20 to 100 glucose units. Despite a wealth of data on short oligosaccharide binding to GHs, no structural evidence is available for their interaction with polymeric substrates that better represent the natural polysaccharide. We have determined the crystal structure of Thermus aquaticus AM in complex with a 34-meric CA-one of the largest carbohydrates resolved by x-ray crystallography and a mimic of the natural polymeric amylose substrate. In total, 15 glucose residues interact with the protein in an extended crevice with a length of more than 40 Å. A modified succinimide, derived from aspartate, mediates protein-sugar interactions, suggesting a biological role for this nonstandard amino acid. The structure, together with functional assays, provides unique insights into the interaction of GHs with their polymeric substrate and reveals a molecular ruler mechanism for minimal ring-size determination of CA products.

U2 - 10.1126/sciadv.1601386

DO - 10.1126/sciadv.1601386

M3 - Article

VL - 3

SP - 1

EP - 10

JO - Science Advances

JF - Science Advances

SN - 2375-2548

IS - 1

M1 - e1601386

ER -