ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 28 citations in OpenAlex.
- Amylosucrase as a Versatile Biocatalyst for Next-Generation Functional Ingredients: Starch Modification and Glycoside Synthesis.Comprehensive reviews in food science and food safety · 2026Review
- Mining and Characterization of Amylosucrase fromInternational journal of molecular sciences · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Identification and characterization of a novel high-activity amylosucrase from Salinispirillum sp. LH10-3-1.Applied microbiology and biotechnology · 2023Article
- Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase.Food science and biotechnology · 2020Review
- The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology.Acta crystallographica. Section F, Structural biology communications · 2017Article
- GH13 amylosucrases and GH70 branching sucrases, atypical enzymes in their respective families.Cellular and molecular life sciences : CMLS · 2016Review
- Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Similarities and differences in the biochemical and enzymological properties of the four isomaltases from Saccharomyces cerevisiae.FEBS open bio · 2014Article
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6 authors at 4 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Amylosucrases (ASes) catalyze the formation of an α-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor α-1,4-glucan. To date, several ligand-bound crystal structures of wild-type and mutant ASes from Neisseria polysaccharea and Deinococcus geothermalis have been solved. These structures all display a very similar overall conformation with a deep pocket leading to the site for transglucosylation, subsite -1. This has led to speculation on how sucrose enters the active site during glucan elongation. In contrast to previous studies, the AS structure from D. radiodurans presented here has a completely empty -1 subsite. This structure is strikingly different from other AS structures, as an active-site-lining loop comprising residues Leu214-Asn225 is found in a previously unobserved conformation. In addition, a large loop harbouring the conserved active-site residues Asp133 and Tyr136 is disordered. The result of the changed loop conformations is that the active-site topology is radically changed, leaving subsite -1 exposed and partially dismantled. This structure provides novel insights into the dynamics of ASes and comprises the first structural support for an elongation mechanism that involves considerable conformational changes to modulate accessibility to the sucrose-binding site and thereby allows successive cycles of glucosyl-moiety transfer to a growing glucan chain.
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