4RBN
The crystal structure of Nitrosomonas europaea sucrose synthase: Insights into the evolutionary origin of sucrose metabolism in prokaryotes
Summary for 4RBN
| Entry DOI | 10.2210/pdb4rbn/pdb |
| Descriptor | Sucrose synthase:Glycosyl transferases group 1 (2 entities in total) |
| Functional Keywords | sucrose synthase, rossmann fold, glucosyltransferase, ndp-glucose, d-fructose, ndp, sucrose, cytosol, transferase |
| Biological source | Nitrosomonas europaea |
| Total number of polymer chains | 4 |
| Total formula weight | 363873.28 |
| Authors | Wu, R.,Asencion Diez, M.D.,Figueroa, C.M.,Machtey, M.,Iglesias, A.A.,Ballicora, M.A.,Liu, D. (deposition date: 2014-09-12, release date: 2015-07-01, Last modification date: 2024-02-28) |
| Primary citation | 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 Cited by 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: 26013491DOI: 10.1128/JB.00110-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.05 Å) |
Structure validation
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