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1o9b

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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:01:21 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:47:07 2007''

Revision as of 13:42, 30 October 2007


1o9b, resolution 2.50Å

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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, ... [(full description)]

About this Structure

1O9B is a [Single protein] structure of sequence from [Escherichia coli] with PO4 and NAD as [ligands]. Active as [Shikimate dehydrogenase], with EC number [1.1.1.25]. Structure known Active Site: NAA. 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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