Structure of l-Serine Dehydratase from Legionella pneumophila: Novel Use of the C-Terminal Cysteine as an Intrinsic Competitive Inhibitor

Abstract

Here we report the first complete structure of a bacterial Fe-S l-serine dehydratase determined to 2.25 Å resolution. The structure is of the type 2 l-serine dehydratase from Legionella pneumophila that consists of a single polypeptide chain containing a catalytic α domain and a β domain that is structurally homologous to the "allosteric substrate binding… (More)
DOI: 10.1021/bi501253w

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