1ldn
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(New page: 200px<br /><applet load="1ldn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ldn, resolution 2.5Å" /> '''STRUCTURE OF A TERNAR...)
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STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
Overview
We report the refined structure of a ternary complex of an allosterically, activated lactate dehydrogenase, including the important active site loop., Eightfold non-crystallographic symmetry averaging was utilized to improve, the density maps. Interactions between the protein and bound coenzyme and, oxamate are described in relation to other studies using site-specific, mutagenesis. Fructose 1,6-bisphosphate (FruP2) is bound to the enzyme, across one of the 2-fold axes of the tetramer, with the two phosphate, moieties interacting with two anion binding sites, one on each of two, subunits, across this interface. However, because FruP2 binds at this, special site, yet does not possess an internal 2-fold symmetry axis, the, ligand is statistically disordered and binds to each site in two different, orientations. Binding of FruP2 to the tetramer is signalled to the active, site principally through two interactions with His188 and Arg173. His188, is connected to His195 (which binds the carbonyl group of the substrate), and Arg173 is connected to Arg171 (the residue that binds the carboxylate, group of the substrate).
About this Structure
1LDN is a Single protein structure of sequence from Geobacillus stearothermophilus with FBP, OXM and NAD as ligands. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution., Wigley DB, Gamblin SJ, Turkenburg JP, Dodson EJ, Piontek K, Muirhead H, Holbrook JJ, J Mol Biol. 1992 Jan 5;223(1):317-35. PMID:1731077
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