Shikimate dehydrogenase structure reveals novel fold.
The structure of shikimate 5-dehydrogenase, the fourth enzyme in the shikimate biosynthesis pathway and a member of a large enzyme family without clear structural peer, reveals a novel topological fold for the substrate binding domain and, through homology modeling, expands the possibilities for antimicrobial and herbicide design.
Vogan
Erik
E
Department of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA.
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D004926:Escherichia coli / Q000201:enzymology; D019143:Evolution, Molecular; D014644:Genetic Variation; D006193:Haemophilus influenzae / Q000201:enzymology; D008024:Ligands; D008837:Micrococcus / Q000201:enzymology / Q000235:genetics; D008958:Models, Molecular; D009249:NADP / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D015203:Reproducibility of Results; D012765:Shikimic Acid / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D008024:Ligands; D012765:Shikimic Acid; D009249:NADP; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase