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Literature summary for 2.4.1.10 extracted from

  • Wuerges, J.; Caputi, L.; Cianci, M.; Boivin, S.; Meijers, R.; Benini, S.
    The crystal structure of Erwinia amylovora levansucrase provides a snapshot of the products of sucrose hydrolysis trapped into the active site (2015), J. Struct. Biol., 191, 290-298.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recobinant expression of N-terminally His6- and GST-tagged enzyme in Escherichia coli Erwinia amylovora

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, mixing of 0.001 ml of 25 mg/ml protein solution containing 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, with 0.001 ml of crystallisation reagent containing 35% PEG 2000 MME, 0.1 M KSCN, X-ray diffraction structure determination and analysis at 2.77 A resolution, molecular replacement using Gluconacetobacter diazotrophicus levansucrase LsdA, PDB ID 1W18, as a search model, enzyme structure comparisons, overview Erwinia amylovora

Organism

Organism UniProt Comment Textmining
Erwinia amylovora Q46654
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Erwinia amylovora ATCC 49946 Q46654
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Subunits

Subunits Comment Organism
More enzyme structure comparisons, overview. The enzyme shows the five-bladed beta-propeller typical of glycoside hydrolase families 32 and 68 members Erwinia amylovora

Synonyms

Synonyms Comment Organism
Lsc
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Erwinia amylovora
SacB
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Erwinia amylovora

General Information

General Information Comment Organism
evolution the enzyme shows the five-bladed beta-propeller typical of glycoside hydrolase families 32 and 68 members Erwinia amylovora
additional information enzyme structure comparisons, overview Erwinia amylovora
physiological function levan is produced by a single enzyme, levansucrase. Levan is required for the formation of a protective biofilm and represents one of several virulence factors of the bacterium Erwinia amylovora