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

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 seque...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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Journal:
Journal of bacteriology
Volume:
185
Issue:
14
Pages:
4144-4151
Publication date:
2003-07-05
DOI:
EISSN:
1098-5530
ISSN:
0021-9193
URN:
uuid:f29c1691-5ee4-403c-ac6b-a514cdf29c7d
Source identifiers:
32401
Local pid:
pubs:32401

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