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Article
Nature Structural Biology  10, 935 - 941 (2003)
Published online: 28 September 2003; | doi:10.1038/nsb974

Structural framework of fructosyl transfer in Bacillus subtilis levansucrase

Guoyu Meng & Klaus Fütterer

School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.

Correspondence should be addressed to Klaus Fütterer K.Futterer@bham.ac.uk
Many bacteria and about 40,000 plant species form primary carbohydrate reserves based on fructan; these polymers of beta-D-fructofuranose are thought to confer tolerance to drought and frost in plants. Microbial fructan, the beta(2,6)-linked levan, is synthesized directly from sucrose by levansucrase, which is able to catalyze both sucrose hydrolysis and levan polymerization. The crystal structure of Bacillus subtilis levansucrase, determined to a resolution of 1.5 Å, shows a rare five-fold beta-propeller topology with a deep, negatively charged central pocket. Arg360, a residue essential for polymerase activity, lies in a solvent-exposed site adjacent to the central pocket. Mutagenesis data and the sucrose-bound structure of inactive levansucrase E342A, at a resolution of 2.1 Å, strongly suggest that three conserved acidic side chains in the central pocket are critical for catalysis, and presumably function as nucleophile (Asp86) and general acid (Glu342), or stabilize the transition state (Asp247).

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REFERENCE
Covalent Nucleophilic Catalysis
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Genetic Engineering: Reporter Genes
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RESEARCH
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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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