Folmer Fredslund, Marine Goux, Bernard Offmann, Marie Demonceaux, Corinne André-Miral, Ditte Welner, David Teze
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引用次数: 0
Abstract
Sucrose phosphorylases are essential enzymes regulating sucrose metabolism, and it has been shown that a loop rearrangement is essential to their catalytic cycle. Crystal structures of only six sucrose phosphorylase enzymes are available. Here, we present the crystal structure of a sucrose phosphorylase from a proteobacterium, Alteromonas mediterranea, at 2.15 Å resolution. The available sucrose phosphorylase structures have shown that an important conformational change occurs during the catalytic cycle or upon mutagenesis. Interestingly, our data present clear indications of the two major conformations in the same crystal.
期刊介绍:
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