1p74
From Proteopedia
(New page: 200px<br /><applet load="1p74" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p74, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1p74.jpg|left|200px]]<br /><applet load="1p74" size=" | + | [[Image:1p74.jpg|left|200px]]<br /><applet load="1p74" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p74, resolution 2.40Å" /> | caption="1p74, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE'''<br /> | '''CRYSTAL STRUCTURE OF SHIKIMATE DEHYDROGENASE (AROE) FROM HAEMOPHILUS INFLUENZAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction | + | 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== | ==About this Structure== | ||
| - | 1P74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] Full crystallographic information is available from [http:// | + | 1P74 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P74 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brooun, A.]] | [[Category: Brooun, A.]] | ||
| - | [[Category: Delft, F | + | [[Category: Delft, F von.]] |
| - | [[Category: Knuth, M | + | [[Category: Knuth, M W.]] |
| - | [[Category: McRee, D | + | [[Category: McRee, D E.]] |
| - | [[Category: Swanson, R | + | [[Category: Swanson, R V.]] |
[[Category: Ye, S.]] | [[Category: Ye, S.]] | ||
[[Category: haemophilus influenzae]] | [[Category: haemophilus influenzae]] | ||
[[Category: shikimate dehydrogenase]] | [[Category: shikimate dehydrogenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:50 2008'' |
Revision as of 12:25, 21 February 2008
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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. Active as Shikimate dehydrogenase, with EC number 1.1.1.25 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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