1l9w
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=[[1qfe|1QFE]], [[1gqn|1GQN]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9w OCA], [http://www.ebi.ac.uk/pdbsum/1l9w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l9w RCSB]</span> | ||
}} | }} | ||
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[[Category: Sawyer, L.]] | [[Category: Sawyer, L.]] | ||
[[Category: Shrive, A K.]] | [[Category: Shrive, A K.]] | ||
| - | [[Category: DHS]] | ||
[[Category: complex with product]] | [[Category: complex with product]] | ||
[[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 22:00:11 2008'' |
Revision as of 19:00, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 3-dehydroquinate dehydratase, with EC number 4.2.1.10 | ||||||
| Related: | 1QFE, 1GQN
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF 3-DEHYDROQUINASE FROM SALMONELLA TYPHI COMPLEXED WITH REACTION PRODUCT
Overview
The type I 3-dehydroquinate dehydratase (DHQase) which catalyses the reversible dehydration of 3-dehydroquinic acid to 3-dehydroshikimic acid is involved in the shikimate pathway for the biosynthesis of aromatic compounds. The shikimate pathway is absent in mammals, which makes structural information about DHQase vital for the rational design of antimicrobial drugs and herbicides. The crystallographic structure of the type I DHQase from Salmonella typhi has now been determined for the native form at 1.78 A resolution (R = 19.9%; R(free) = 24.7%). The structure of the modified enzyme to which the product has been covalently bound has also been determined but in a different crystal form (2.1 A resolution; R = 17.7%; R(free) = 24.5%). An analysis of the three available crystal forms has provided information about the physiological dimer interface. The enzyme relies upon the closure of a lid-like loop to complete its active site. As the lid-loop tends to stay in the closed position, dimerization appears to play a role in biasing the arrangement of the loop towards its open position, thus facilitating substrate access.
About this Structure
1L9W is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.
Reference
Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity., Lee WH, Perles LA, Nagem RA, Shrive AK, Hawkins A, Sawyer L, Polikarpov I, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):798-804. Epub 2002, Apr 26. PMID:11976491
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