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- W2060658515 abstract "Ornithine decarboxylase fromLactobacillus30a (L30a OrnDC) is representative of the large, pyridoxal-5′-phosphate-dependent decarboxylases that act on lysine, arginine or ornithine. The crystal structure of the L30a OrnDC has been solved to 3.0 Å resolution using MIR phases in combination with density modification (space groupp6;a= 195.6 Å,c= 97.6 Å; dimer of 1460 amino acid residues/asymmetric unit;Vm= 3.26 Å3/Da). The refined crystallographicR-value was 0.219 (Rfree= 0.268) using 2-fold restraints with a 4σ cutoff and 8.0 to 3.0 Å resolution data. Six dimers related by C6 symmetry compose the enzymatically active dodecamer (∼ 106Da). Each monomer of L30a OrnDC can be described in terms of five sequential folding domains. The amino-terminal domain, residues 1 to 107, consists of a five-stranded β-sheet termed the “wing” domain. Two wing domains of each dimer project inward towards the center of the dodecamer and contribute to dodecamer stabilization. The “linker” domain, residues 108 to 160, consists of short α-helices separated by a loop that fills in the PLP packet. The third domain, residues 161 to 413, is an α/β domain containing a seven stranded β-sheet that resembles the PLP-binding domain of the aspartate aminotransferases. The fourth domain, residues 414 to 569, resembles the “small” domain of the aspartate aminotransferases, but is significantly larger due to insertions. The remaining carboxy-terminal domain, residues 570 to 730, is organized into multiple antiparallel loops and seven α-helices that help form a deep channel leading to the PLP-binding site." @default.
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- W2060658515 date "1995-10-01" @default.
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- W2060658515 title "Crystallographic Structure of a PLP-Dependent Ornithine Decarboxylase fromLactobacillus30a to 3.0 Å Resolution" @default.
- W2060658515 doi "https://doi.org/10.1006/jmbi.1995.0526" @default.
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