1qfe
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DHS:3-AMINO-4,5-DIHYDROXY-CYCLOHEX-1-ENECARBOXYLATE'>DHS</scene> | |LIGAND= <scene name='pdbligand=DHS:3-AMINO-4,5-DIHYDROXY-CYCLOHEX-1-ENECARBOXYLATE'>DHS</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfe OCA], [http://www.ebi.ac.uk/pdbsum/1qfe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfe RCSB]</span> | ||
}} | }} | ||
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[[Category: Sawyer, L.]] | [[Category: Sawyer, L.]] | ||
[[Category: Shrive, A K.]] | [[Category: Shrive, A K.]] | ||
| - | [[Category: DHS]] | ||
[[Category: 3rd enzyme in the shikimate pathway]] | [[Category: 3rd enzyme in the shikimate pathway]] | ||
[[Category: conversion of 3-dehydroquinate to dehydroshikimate]] | [[Category: conversion of 3-dehydroquinate to dehydroshikimate]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:42 2008'' |
Revision as of 20:12, 30 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 3-dehydroquinate dehydratase, with EC number 4.2.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF TYPE I 3-DEHYDROQUINATE DEHYDRATASE FROM SALMONELLA TYPHI
Overview
The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well conserved as are their catalytic mechanisms. The two types of 3-dehydroquinate dehydratase (DHQase) are therefore most unusual since they are unrelated at the sequence level and they utilize completely different mechanisms to catalyze the same overall reaction. The type I enzymes catalyze a cis-dehydration of 3-dehydroquinate via a covalent imine intermediate, while the type II enzymes catalyze a trans-dehydration via an enolate intermediate. Here we report the three-dimensional structures of a representative member of each type of biosynthetic DHQase. Both enzymes function as part of the shikimate pathway, which is essential in microorganisms and plants for the biosynthesis of aromatic compounds including folate, ubiquinone and the aromatic amino acids. An explanation for the presence of two different enzymes catalyzing the same reaction is presented. The absence of the shikimate pathway in animals makes it an attractive target for antimicrobial agents. The availability of these two structures opens the way for the design of highly specific enzyme inhibitors with potential importance as selective therapeutic agents.
About this Structure
1QFE is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.
Reference
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction., Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L, Nat Struct Biol. 1999 Jun;6(6):521-5. PMID:10360352
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