1iyu
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(New page: 200px<br /> <applet load="1iyu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iyu" /> '''LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COM...)
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Revision as of 17:43, 29 October 2007
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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 ... [(full description)]
About this Structure
1IYU is a [Single protein] structure of sequence from [Azotobacter vinelandii]. Active as [[1]], with EC number [2.3.1.12]. 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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