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Crystal structures of peptide deformylase from S. aureus in complex with novel inhibitors are presented together with their functional analysis. A detailed comparative analysis of these structures as well as the activities of the inhibitors allowed the elucidation of distinctive structural changes which depend upon the class of inhibitor.

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The structures of apo and holo mutants of alginate lyase A1-III revealed a large open/closed conformational change of lid loop. The closed lid loop is involved both in the binding of substrate and catalysis of the enzyme.
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