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1p74
From Proteopedia
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[[Image:1p74.jpg|left|200px]] | [[Image:1p74.jpg|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE''' | '''CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE''' | ||
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[[Category: Swanson, R V.]] | [[Category: Swanson, R V.]] | ||
[[Category: Ye, S.]] | [[Category: Ye, S.]] | ||
| - | [[Category: | + | [[Category: Haemophilus influenzae]] |
| - | [[Category: | + | [[Category: Shikimate dehydrogenase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:46:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:46, 3 May 2008
CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE
Overview
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.
About this Structure
1P74 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode., Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE, J Bacteriol. 2003 Jul;185(14):4144-51. PMID:12837789 Page seeded by OCA on Sat May 3 04:46:09 2008
