1P77

CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE

Summary for 1P77

• Entry DOI: 10.2210/pdb1p77/pdb
• Related: 1P74
• Descriptor: Shikimate 5-dehydrogenase, ACETATE ION, 2'-MONOPHOSPHOADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: shikimate dehydrogenase, haemophilus influenzae, nadph, oxidoreductase
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 1
• Total formula weight: 30354.23

Authors

Ye, S.,von Delft, F.,Brooun, A.,Knuth, M.W.,Swanson, R.V.,McRee, D.E. (deposition date: 2003-04-30, release date: 2003-08-12, Last modification date: 2023-08-16)

Primary citation

Ye, S.,von Delft, F.,Brooun, A.,Knuth, M.W.,Swanson, R.V.,McRee, D.E.
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode
J.Bacteriol., 185:4144-4151, 2003

PubMed Abstract: 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 sequence motif, GAGGXX, that results in NADPH adopting a nonstandard binding mode with the nicotinamide and ribose moieties disordered in the binary complex. A deep pocket with a narrow entrance between the two domains, containing strictly conserved residues primarily contributed by the catalytic domain, is identified as a potential 3-dehydroshikimate binding pocket. The flexibility of the nicotinamide mononucleotide portion of NADPH may be necessary for the substrate 3-dehydroshikimate to enter the pocket and for the release of the product shikimate.

PubMed: 12837789
DOI: 10.1128/JB.185.14.4144-4151.2003

Experimental method

X-RAY DIFFRACTION (1.95 Å)