The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology

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The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology. / Skov, Lars K; Pizzut-Serin, Sandra; Remaud-Simeon, Magali; Ernst, Heidi A; Gajhede, Michael; Mirza, Osman Asghar.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. 69, No. Pt 9, 09.2013, p. 973-8.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Skov, LK, Pizzut-Serin, S, Remaud-Simeon, M, Ernst, HA, Gajhede, M & Mirza, OA 2013, 'The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, vol. 69, no. Pt 9, pp. 973-8. https://doi.org/10.1107/S1744309113021714

APA

Skov, L. K., Pizzut-Serin, S., Remaud-Simeon, M., Ernst, H. A., Gajhede, M., & Mirza, O. A. (2013). The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 69(Pt 9), 973-8. https://doi.org/10.1107/S1744309113021714

Vancouver

Skov LK, Pizzut-Serin S, Remaud-Simeon M, Ernst HA, Gajhede M, Mirza OA. The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2013 Sep;69(Pt 9):973-8. https://doi.org/10.1107/S1744309113021714

Author

Skov, Lars K ; Pizzut-Serin, Sandra ; Remaud-Simeon, Magali ; Ernst, Heidi A ; Gajhede, Michael ; Mirza, Osman Asghar. / The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology. In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2013 ; Vol. 69, No. Pt 9. pp. 973-8.

Bibtex

@article{d6a0b6c38c9641e1b053270f779af687,
title = "The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology",
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.",
author = "Skov, {Lars K} and Sandra Pizzut-Serin and Magali Remaud-Simeon and Ernst, {Heidi A} and Michael Gajhede and Mirza, {Osman Asghar}",
year = "2013",
month = "9",
doi = "10.1107/S1744309113021714",
language = "English",
volume = "69",
pages = "973--8",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 9",

}

RIS

TY - JOUR

T1 - The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology

AU - Skov, Lars K

AU - Pizzut-Serin, Sandra

AU - Remaud-Simeon, Magali

AU - Ernst, Heidi A

AU - Gajhede, Michael

AU - Mirza, Osman Asghar

PY - 2013/9

Y1 - 2013/9

N2 - 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.

AB - 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.

U2 - 10.1107/S1744309113021714

DO - 10.1107/S1744309113021714

M3 - Journal article

VL - 69

SP - 973

EP - 978

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 9

ER -

ID: 50816371