Document Type

Article

Publication Date

5-2015

Publication Title

Journal of Bacteriology

Pages

1-54

Publisher Name

American Society for Microbiology

Abstract

In this paper we report the first crystal structure of a prokaryotic sucrose synthase from the non-photosynthetic bacterium Nitrosomonas europaea. The obtained structure was in an open form, whereas the only other available structure from the plant Arabidopsis thaliana was in a closed conformation. Comparative structural analysis revealed a “hinge-latch” combination, which is critical to transition between the open and closed forms of the enzyme. The N. europaea sucrose synthase shares the same fold as the GT-B family of the retaining glycosyltransferases. In addition, a triad of conserved homologous catalytic residues in the family showed to be functionally critical in the N. europaea sucrose synthase (Arg567, Lys572, Glu663). This implies that sucrose synthase shares not only a common origin with the GT-B family, but also a similar catalytic mechanism. The enzyme preferred transferring glucose from ADP-glucose rather than UDP-glucose like the eukaryotic counterparts. This predicts that these prokaryotic organisms have a different sucrose metabolic scenario from plants. Nucleotide preference determines where the glucose moiety is targeted after sucrose is degraded.

Comments

Author Posting. © American Society for Microbiology, 2015. This article is posted here by permission of the American Society for Microbiology for personal use, not for redistribution. The article was published in the Journal of Bacteriology, 2015, http://dx.doi.org/10.1128/JB.00110-15

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This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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