6RV5
X-ray structure of the levansucrase from Erwinia tasmaniensis in complex with levanbiose
Summary for 6RV5
| Entry DOI | 10.2210/pdb6rv5/pdb |
| Related PRD ID | PRD_900051 |
| Descriptor | Levansucrase (Beta-D-fructofuranosyl transferase), beta-D-fructofuranose-(2-6)-beta-D-fructofuranose, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | levansucrase, levanbiose, fructosyltransferase, fructans production., transferase |
| Biological source | Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99) |
| Total number of polymer chains | 1 |
| Total formula weight | 47625.38 |
| Authors | Polsinelli, I.,Caliandro, R.,Demitri, N.,Benini, S. (deposition date: 2019-05-31, release date: 2020-04-01, Last modification date: 2024-01-31) |
| Primary citation | Polsinelli, I.,Caliandro, R.,Demitri, N.,Benini, S. The Structure of Sucrose-Soaked Levansucrase Crystals fromErwinia tasmaniensisreveals a Binding Pocket for Levanbiose. Int J Mol Sci, 21:-, 2019 Cited by PubMed Abstract: Given its potential role in the synthesis of novel prebiotics and applications in the pharmaceutical industry, a strong interest has developed in the enzyme levansucrase (LSC, EC 2.4.1.10). LSC catalyzes both the hydrolysis of sucrose (or sucroselike substrates) and the transfructosylation of a wide range of acceptors. LSC from the Gram-negative bacterium (EtLSC) is an interesting biocatalyst due to its high-yield production of fructooligosaccharides (FOSs). In order to learn more about the process of chain elongation, we obtained the crystal structure of EtLSC in complex with levanbiose (LBS). LBS is an FOS intermediate formed during the synthesis of longer-chain FOSs and levan. Analysis of the LBS binding pocket revealed that its structure was conserved in several related species. The binding pocket discovered in this crystal structure is an ideal target for future mutagenesis studies in order to understand its biological relevance and to engineer LSCs into tailored products. PubMed: 31877648DOI: 10.3390/ijms21010083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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