4RBN

The crystal structure of Nitrosomonas europaea sucrose synthase: Insights into the evolutionary origin of sucrose metabolism in prokaryotes

4RBN の概要

• エントリーDOI: 10.2210/pdb4rbn/pdb
• 分子名称: Sucrose synthase:Glycosyl transferases group 1 (2 entities in total)
• 機能のキーワード: sucrose synthase, rossmann fold, glucosyltransferase, ndp-glucose, d-fructose, ndp, sucrose, cytosol, transferase
• 由来する生物種: Nitrosomonas europaea
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 363873.28

構造登録者

Wu, R.,Asencion Diez, M.D.,Figueroa, C.M.,Machtey, M.,Iglesias, A.A.,Ballicora, M.A.,Liu, D. (登録日: 2014-09-12, 公開日: 2015-07-01, 最終更新日: 2024-02-28)

主引用文献

Wu, R.,Asencion Diez, M.D.,Figueroa, C.M.,Machtey, M.,Iglesias, A.A.,Ballicora, M.A.,Liu, D.
The Crystal Structure of Nitrosomonas europaea Sucrose Synthase Reveals Critical Conformational Changes and Insights into Sucrose Metabolism in Prokaryotes.
J.Bacteriol., 197:2734-2746, 2015

PubMed Abstract: In this paper we report the first crystal structure of a prokaryotic sucrose synthase from the nonphotosynthetic 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 was shown to be functionally critical in the N. europaea sucrose synthase (Arg567, Lys572, and 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.

PubMed: 26013491
DOI: 10.1128/JB.00110-15

実験手法

X-RAY DIFFRACTION (3.05 Å)