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Modeling of the spatial structure of eukaryotic ornithine decarboxylases
Author(s) -
Grishin Nick V.,
Phillips Margaret A.,
Goldsmith Elizabeth J.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040705
Subject(s) - ornithine decarboxylase , biochemistry , ornithine decarboxylase antizyme , enzyme , cofactor , ornithine , pyridoxal phosphate , pyridoxal , chemistry , binding site , stereochemistry , peptide sequence , protein structure , alanine , active site , amino acid , biology , arginine , gene
We used sequence and structural comparisons to determine the fold for eukaryotic ornithine decarboxylase, which we found is related to alanine racemase. These enzymes have no detectable sequence identity with any protein of known structure, including three pyridoxal phosphate‐utilizing enzymes. Our studies suggest that the N‐terminal domain of ornithine decarboxylase folds into a β/α‐barrel. Through the analysis of known barrel structures we developed a topographic model of the pyridoxal phosphate‐binding domain of ornithine decarboxylase, which predicts that the Schiff base lysine and a conserved glycine‐rich sequence both map to the C‐termini of the β‐strands. Other residues in this domain that are likely to have essential roles in catalysis, substrate, and cofactor binding were also identified, suggesting that this model will be a suitable guide to mutagenic analysis of the enzyme mechanism.