1o9b

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[[Image:1o9b.gif|left|200px]]<br /><applet load="1o9b" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1o9b.gif|left|200px]]
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caption="1o9b, resolution 2.50&Aring;" />
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'''QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH'''<br />
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{{Structure
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|PDB= 1o9b |SIZE=350|CAPTION= <scene name='initialview01'>1o9b</scene>, resolution 2.50&Aring;
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|SITE= <scene name='pdbsite=NAA:Po4+Binding+Site+For+Chain+B'>NAA</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1O9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Site: <scene name='pdbsite=NAA:Po4+Binding+Site+For+Chain+B'>NAA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9B OCA].
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1O9B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9B OCA].
==Reference==
==Reference==
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Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities., Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ, J Biol Chem. 2003 May 23;278(21):19463-72. Epub 2003 Mar 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12637497 12637497]
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Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities., Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ, J Biol Chem. 2003 May 23;278(21):19463-72. Epub 2003 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12637497 12637497]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Shikimate dehydrogenase]]
[[Category: Shikimate dehydrogenase]]
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[[Category: quinate]]
[[Category: quinate]]
[[Category: shikimate]]
[[Category: shikimate]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:07:35 2008''

Revision as of 11:07, 20 March 2008

Image:1o9b.gif


PDB ID 1o9b

Drag the structure with the mouse to rotate
, resolution 2.50Å
Sites:
Ligands: and
Activity: Shikimate dehydrogenase, with EC number 1.1.1.25
Coordinates: save as pdb, mmCIF, xml



QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH


Overview

Shikimate dehydrogenase catalyzes the fourth step of the shikimate pathway, the essential route for the biosynthesis of aromatic compounds in plants and microorganisms. Absent in metazoans, this pathway is an attractive target for nontoxic herbicides and drugs. Escherichia coli expresses two shikimate dehydrogenase paralogs, the NADP-specific AroE and a putative enzyme YdiB. Here we characterize YdiB as a dual specificity quinate/shikimate dehydrogenase that utilizes either NAD or NADP as a cofactor. Structures of AroE and YdiB with bound cofactors were determined at 1.5 and 2.5 A resolution, respectively. Both enzymes display a similar architecture with two alpha/beta domains separated by a wide cleft. Comparison of their dinucleotide-binding domains reveals the molecular basis for cofactor specificity. Independent molecules display conformational flexibility suggesting that a switch between open and closed conformations occurs upon substrate binding. Sequence analysis and structural comparison led us to propose the catalytic machinery and a model for 3-dehydroshikimate recognition. Furthermore, we discuss the evolutionary and metabolic implications of the presence of two shikimate dehydrogenases in E. coli and other organisms.

About this Structure

1O9B is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities., Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ, J Biol Chem. 2003 May 23;278(21):19463-72. Epub 2003 Mar 12. PMID:12637497

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