2c8m
From Proteopedia
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STRUCTURE OF PROTEIN TA0514, PUTATIVE LIPOATE PROTEIN LIGASE FROM T. ACIDOPHILUM WITH BOUND LIPOIC ACID
Overview
Lipoyl-lysine swinging arms are crucial to the reactions catalysed by the, 2-oxo acid dehydrogenase multienzyme complexes. A gene encoding a putative, lipoate protein ligase (LplA) of Thermoplasma acidophilum was cloned and, expressed in Escherichia coli. The recombinant protein, a monomer of, molecular mass 29 kDa, was catalytically inactive. Crystal structures in, the absence and presence of bound lipoic acid were solved at 2.1 A, resolution. The protein was found to fall into the alpha/beta class and to, be structurally homologous to the catalytic domains of class II, aminoacyl-tRNA synthases and biotin protein ligase, BirA. Lipoic acid in, LplA was bound in the same position as biotin in BirA. The structure of, the T.acidophilum LplA and limited proteolysis of E.coli LplA together, ... [(full description)]
About this Structure
2C8M is a [Single protein] structure of sequence from [Thermoplasma acidophilum] with LPA as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification., McManus E, Luisi BF, Perham RN, J Mol Biol. 2006 Feb 24;356(3):625-37. Epub 2005 Dec 5. PMID:16384580
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