1npy
From Proteopedia
(New page: 200px<br /><applet load="1npy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npy, resolution 1.75Å" /> '''Structure of shikima...) |
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| - | [[Image:1npy.gif|left|200px]]<br /><applet load="1npy" size=" | + | [[Image:1npy.gif|left|200px]]<br /><applet load="1npy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1npy, resolution 1.75Å" /> | caption="1npy, resolution 1.75Å" /> | ||
'''Structure of shikimate 5-dehydrogenase-like protein HI0607'''<br /> | '''Structure of shikimate 5-dehydrogenase-like protein HI0607'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To date two classes of shikimate dehydrogenases have been identified and | + | To date two classes of shikimate dehydrogenases have been identified and characterized, YdiB and AroE. YdiB is a bifunctional enzyme that catalyzes the reversible reductions of dehydroquinate to quinate and dehydroshikimate to shikimate in the presence of either NADH or NADPH. In contrast, AroE catalyzes the reversible reduction of dehydroshikimate to shikimate in the presence of NADPH. Here we report the crystal structure and biochemical characterization of HI0607, a novel class of shikimate dehydrogenase annotated as shikimate dehydrogenase-like. The kinetic properties of HI0607 are remarkably different from those of AroE and YdiB. In comparison with YdiB, HI0607 catalyzes the oxidation of shikimate but not quinate. The turnover rate for the oxidation of shikimate is approximately 1000-fold lower compared with that of AroE. Phylogenetic analysis reveals three independent clusters representing three classes of shikimate dehydrogenases, namely AroE, YdiB, and this newly characterized shikimate dehydrogenase-like protein. In addition, mutagenesis studies of two invariant residues, Asp-103 and Lys-67, indicate that they are important catalytic groups that may function as a catalytic pair in the shikimate dehydrogenase reaction. This is the first study that describes the crystal structure as well as mutagenesis and mechanistic analysis of this new class of shikimate dehydrogenase. |
==About this Structure== | ==About this Structure== | ||
| - | 1NPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Korolev, S.]] | [[Category: Korolev, S.]] | ||
[[Category: Koroleva, O.]] | [[Category: Koroleva, O.]] | ||
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Zarembinski, T.]] | [[Category: Zarembinski, T.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:47 2008'' |
Revision as of 12:08, 21 February 2008
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Structure of shikimate 5-dehydrogenase-like protein HI0607
Overview
To date two classes of shikimate dehydrogenases have been identified and characterized, YdiB and AroE. YdiB is a bifunctional enzyme that catalyzes the reversible reductions of dehydroquinate to quinate and dehydroshikimate to shikimate in the presence of either NADH or NADPH. In contrast, AroE catalyzes the reversible reduction of dehydroshikimate to shikimate in the presence of NADPH. Here we report the crystal structure and biochemical characterization of HI0607, a novel class of shikimate dehydrogenase annotated as shikimate dehydrogenase-like. The kinetic properties of HI0607 are remarkably different from those of AroE and YdiB. In comparison with YdiB, HI0607 catalyzes the oxidation of shikimate but not quinate. The turnover rate for the oxidation of shikimate is approximately 1000-fold lower compared with that of AroE. Phylogenetic analysis reveals three independent clusters representing three classes of shikimate dehydrogenases, namely AroE, YdiB, and this newly characterized shikimate dehydrogenase-like protein. In addition, mutagenesis studies of two invariant residues, Asp-103 and Lys-67, indicate that they are important catalytic groups that may function as a catalytic pair in the shikimate dehydrogenase reaction. This is the first study that describes the crystal structure as well as mutagenesis and mechanistic analysis of this new class of shikimate dehydrogenase.
About this Structure
1NPY is a Single protein structure of sequence from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae., Singh S, Korolev S, Koroleva O, Zarembinski T, Collart F, Joachimiak A, Christendat D, J Biol Chem. 2005 Apr 29;280(17):17101-8. Epub 2005 Feb 25. PMID:15735308
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