Crystal Structure of Saccharopine Reductase from Magnaporthe grisea, an Enzyme of the α-Aminoadipate Pathway of Lysine Biosynthesis Eva Johansson, James.

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Presentation transcript:

Crystal Structure of Saccharopine Reductase from Magnaporthe grisea, an Enzyme of the α-Aminoadipate Pathway of Lysine Biosynthesis Eva Johansson, James J. Steffens, Ylva Lindqvist, Gunter Schneider Structure Volume 8, Issue 10, Pages 1037-1047 (October 2000) DOI: 10.1016/S0969-2126(00)00512-8

Figure 1 Overview of the α-Aminoadipate Pathway of Lysine Biosynthesis The reaction catalysed by saccharopine reductase is shown boxed Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 2 The Fold of Saccharopine Reductase Domain I is shown in blue, domain II in red and domain III in green. Ribbon views of (a) the domains and (b) the subunit. The bound NADPH and the product are shown in ball-and-stick representation. (c) A topology diagram of saccharopine reductase Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 3 Conformational Differences in the Observed Crystal Structures of Saccharopine Reductase Superposition of the Cα traces of apo saccharopine reductase (space group C2; magenta), apo saccharopine reductase (space group C2221; cyan), and the ternary complex (space group P21; yellow). The arrow points to areas of local structural differences in domain II Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 4 Active Site of Saccharopine Reductase (a) Difference electron densities for the bound ligands, NADPH, and saccharopine, in the ternary complex with saccharopine reductase. The 2Fo–Fc difference electron-density map is contoured at 1.2σ. (b) Stereoview of the active site of saccharopine reductase. Hydrogen bonds are indicated by dashed lines Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 5 Amino Acid Sequence of Saccharopine Reductase from M. grisea Secondary-structure elements are marked as arrows (β strands) and filled rectangles (helices). The secondary-structure elements are colour-coded: domain I, blue; domain II, red; and domain III, green. Residues completely conserved in M. grisea, Saccharomyces cerevisiae, Schizoaccharomyces pombe, Brassica napus (fragment), Arabidopsis thaliana, Caenorhabditis elegans, Homo sapiens, and Mus musculus are shown in red. Residues only conserved in the fungal enzymes are shown in blue Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 6 Interactions of the Bound Ligands with Protein Atoms at the Active Site of Saccharopine Reductase Dotted lines indicate hydrogen bonds, and red rays show hydrophobic interactions. Invariant residues are marked by an asterisk. (a) The NADPH-binding site and (b) the saccharopine-binding site. Atoms are shown in standard colours Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)

Figure 7 Proposed Mechanism of the Reaction Catalysed by Saccharopine Reductase Structure 2000 8, 1037-1047DOI: (10.1016/S0969-2126(00)00512-8)