6FRW

X-ray structure of the levansucrase from Erwinia tasmaniensis

Summary for 6FRW

• Entry DOI: 10.2210/pdb6frw/pdb
• Descriptor: Levansucrase (Beta-D-fructofuranosyl transferase), GLYCEROL, ZINC ION, ... (4 entities in total)
• Functional Keywords: fructosyltransferase, sucrose hydrolase, fructans production, transferase
• Biological source: Erwinia tasmaniensis
• Total number of polymer chains: 1
• Total formula weight: 46832.95

Authors

Polsinelli, I.,Salomone-Stagni, M.,Caliandro, R.,Demitri, N.,Benini, S. (deposition date: 2018-02-16, release date: 2019-02-06, Last modification date: 2024-05-08)

Primary citation

Polsinelli, I.,Caliandro, R.,Salomone-Stagni, M.,Demitri, N.,Rejzek, M.,Field, R.A.,Benini, S.
Comparison of the Levansucrase from the epiphyte Erwinia tasmaniensis vs its homologue from the phytopathogen Erwinia amylovora.
Int. J. Biol. Macromol., 127:496-501, 2019

PubMed Abstract: Erwinia tasmaniensis is an epiphytic bacterium related to the plant pathogen Erwinia amylovora, the etiological agent of fire blight. In this study the levansucrase from E. tasmaniensis (EtLsc) has been compared with the homologous enzyme from E. amylovora (EaLsc). We characterized the enzymatic activity and compared the products profile of both enzymes by High Performance Anion Exchange Chromatography coupled with Pulsed Amperometric Detector (HPAEC-PAD). Moreover we determined the crystal structure of EtLsc to understand the structural peculiarity causing the different product profiles of the two homologues. EtLsc exhibits increased efficiency in the production of FOS, resulting in a better catalyst for biotechnological synthesis than EaLsc. Based on our results, we propose that the role of this enzyme in the life cycle of the two bacteria is most likely related to survival, rather than linked to pathogenicity in E. amylovora.

PubMed: 30660564
DOI: 10.1016/j.ijbiomac.2019.01.074

Experimental method

X-RAY DIFFRACTION (1.52 Å)