1qjo
From Proteopedia
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INNERMOST LIPOYL DOMAIN OF THE PYRUVATE DEHYDROGENASE FROM ESCHERICHIA COLI
Overview
The three lipoyl (E2plip) domains of the dihydrolipoyl acetyltransferase, component of the pyruvate dehydrogenase (PDH) complex of Escherichia coli, house the lipoyl-lysine side chain essential for active-site coupling and, substrate channelling within the complex. The structure of the, unlipoylated form of the innermost domain (E2plip(apo)) was determined by, multidimensional NMR spectroscopy and found to resemble closely that of a, nonfunctional hybrid domain determined previously [Green et al. (1995) J., Mol. Biol. 248, 328-343]. The domain comprises two four-stranded, beta-sheets, with the target lysine residue residing at the tip of a, type-I beta-turn in one of the sheets; the N- and C-termini lie close, together at the opposite end of the molecule in the other beta-sheet., ... [(full description)]
About this Structure
1QJO is a [Single protein] structure of sequence from [Escherichia coli]. Full crystallographic information is available from [OCA].
Reference
Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli., Jones DD, Stott KM, Howard MJ, Perham RN, Biochemistry. 2000 Jul 25;39(29):8448-59. PMID:10913250
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