English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Amylose recognition and ring-size determination of amylomaltase

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

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0000-1693-1 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-16A4-E
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Roth, Christian1, Author              
Weizenmann, Nicole, Author
Bexten, Nicola, Author
Saenger, Wolfram, Author
Zimmermann, Wolfgang, Author
Maier, Timm, Author
Sträter, Norbert, Author
Affiliations:
1External Organizations, ou_persistent22              

Content

show
hide
Free keywords: -
 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 {˚ A. 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.

Details

show
hide
Language(s):
 Dates: 2017
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1126/sciadv.1601386
BibTex Citekey: Rothe1601386
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 3 (1) Sequence Number: e1601386 Start / End Page: - Identifier: ISSN: 2375-2548