The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.

Journal article

Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate. We report the first X-ray structure of shikimate dehydrogenase from Haemophilus influenzae to 2.4-A resolution and its complex with NADPH to 1.95-A resolution. The molecule contains two domains, a catalytic domain with a novel open twisted alpha/beta motif and an NADPH binding domain with a typical Rossmann fold. The enzyme contains a unique glycine-rich P-loop with a conserved seque...

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Authors: Ye, S; von Delft, F; Brooun, A; Knuth, M; Swanson, R

• Publication status: Published
• Journal: Journal of bacteriology
• Volume: 185
• Issue: 14
• Pages: 4144-4151
• Publication date: 2003-07-01
• DOI: 10.1128/jb.185.14.4144-4151.2003
• EISSN: 1098-5530
• ISSN: 0021-9193
• Language: English
• Keywords: Protein Conformation; Binding Sites; Catalytic Domain; Alcohol Oxidoreductases; Sequence Alignment; Protein Structure, Tertiary; Crystallography, X-Ray; Models, Molecular; NADP; Humans; Haemophilus influenzae; Molecular Sequence Data; Amino Acid Sequence; Shikimic Acid