1iyu
From Proteopedia
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LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The three-dimensional structure of the N-terminal lipoyl domain of the, acetyltransferase component of the pyruvate dehydrogenase complex from, Azotobacter vinelandii has been determined using heteronuclear, multidimensional NMR spectroscopy and dynamical simulated annealing. The, structure is compared with the solution structure of the lipoyl domain of, the A. vinelandii 2-oxoglutarate dehydrogenase complex. The overall fold, of the two structures, described as a beta-barrel-sandwich hybrid, is very, similar. This agrees well with the high similarity of NMR-derived, parameters, e.g. chemical shifts, between the two lipoyl domains. The main, structural differences between the two lipoyl domains occur in a, solvent-exposed loop close in space to the lipoylation site. Despite their, high structural similarity, these lipoyl domains show a high preference, for being reductively acylated by their parent 2-oxo acid dehydrogenase., Potential residues of the lipoyl domain involved in this process of, molecular recognition are discussed.
About this Structure
1IYU is a Single protein structure of sequence from Azotobacter vinelandii. Active as Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 Structure known Active Site: LIP. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii., Berg A, Vervoort J, de Kok A, Eur J Biochem. 1997 Mar 1;244(2):352-60. PMID:9119000
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