1p74: Difference between revisions

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[[Image:1p74.jpg|left|200px]]
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{{STRUCTURE_1p74|  PDB=1p74  |  SCENE=  }}  
{{STRUCTURE_1p74|  PDB=1p74  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE'''
===CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Shikimate dehydrogenase]]
[[Category: Shikimate dehydrogenase]]
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Revision as of 21:01, 28 July 2008

File:1p74.png

Template:STRUCTURE 1p74

CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE

Template:ABSTRACT PUBMED 12837789

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

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