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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I03-Macromolecular Crystallography	Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae Halina R. Novak , Christopher Sayer , Misha Isupov , Dorothee Gotz , Andrew Mearns Spragg , Jennifer Littlechild Febs Letters 588 (9), 1616 - 1622 DOI: 10.1016/j.febslet.2014.02.056 PMID: 24613925 Diamond Proposal Number(s): [8889, 6851] Show Abstract ▼ Abstract: A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di-halogenated substrates.	May 2014

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