1nyt
From Proteopedia
(New page: 200px<br /><applet load="1nyt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nyt, resolution 1.50Å" /> '''SHIKIMATE DEHYDROGEN...) |
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| - | [[Image:1nyt.jpg|left|200px]]<br /><applet load="1nyt" size=" | + | [[Image:1nyt.jpg|left|200px]]<br /><applet load="1nyt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nyt, resolution 1.50Å" /> | caption="1nyt, resolution 1.50Å" /> | ||
'''SHIKIMATE DEHYDROGENASE AroE COMPLEXED WITH NADP+'''<br /> | '''SHIKIMATE DEHYDROGENASE AroE COMPLEXED WITH NADP+'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Shikimate dehydrogenase catalyzes the fourth step of the shikimate | + | 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== | ==About this Structure== | ||
| - | 1NYT 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 SO4, NAP and DTV 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] Full crystallographic information is available from [http:// | + | 1NYT 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=SO4:'>SO4</scene>, <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=DTV:'>DTV</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Shikimate dehydrogenase]] | [[Category: Shikimate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lapthorn, A | + | [[Category: Lapthorn, A J.]] |
| - | [[Category: Roszak, A | + | [[Category: Roszak, A W.]] |
[[Category: DTV]] | [[Category: DTV]] | ||
[[Category: NAP]] | [[Category: NAP]] | ||
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[[Category: wide cleft separation]] | [[Category: wide cleft separation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:32 2008'' |
Revision as of 12:11, 21 February 2008
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SHIKIMATE DEHYDROGENASE AroE COMPLEXED WITH NADP+
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
1NYT is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Shikimate dehydrogenase, with EC number 1.1.1.25 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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