1gu1
From Proteopedia
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|PDB= 1gu1 |SIZE=350|CAPTION= <scene name='initialview01'>1gu1</scene>, resolution 1.80Å | |PDB= 1gu1 |SIZE=350|CAPTION= <scene name='initialview01'>1gu1</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=FAA:Fa1+Binding+Site+For+Chain+L'>FAA</scene> | |SITE= <scene name='pdbsite=FAA:Fa1+Binding+Site+For+Chain+L'>FAA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FA1:2,3+-ANHYDRO-QUINIC+ACID'>FA1</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | + | |LIGAND= <scene name='pdbligand=FA1:2,3+-ANHYDRO-QUINIC+ACID'>FA1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | + | |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=1gu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu1 OCA], [http://www.ebi.ac.uk/pdbsum/1gu1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gu1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Robinson, D A.]] | [[Category: Robinson, D A.]] | ||
[[Category: Roszak, A W.]] | [[Category: Roszak, A W.]] | ||
| - | [[Category: FA1]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: TLA]] | ||
| - | [[Category: TRS]] | ||
[[Category: dodecameric quaternary structure]] | [[Category: dodecameric quaternary structure]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
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[[Category: type ii dehydroquinase]] | [[Category: type ii dehydroquinase]] | ||
| - | ''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 20:51:14 2008'' |
Revision as of 17:51, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | 3-dehydroquinate dehydratase, with EC number 4.2.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH 2,3-ANYDRO-QUINIC ACID
Overview
The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high resolution in complexes with a number of ligands, including dehydroshikimate and a rationally designed transition state analogue, 2,3-anhydro-quinic acid. These structures define the active site of the enzyme and the role of key amino acid residues and provide snap shots of the catalytic cycle. The resolution of the flexible lid domain (residues 21-31) shows that the invariant residues Arg23 and Tyr28 close over the active site cleft. The tyrosine acts as the base in the initial proton abstraction, and evidence is provided that the reaction proceeds via an enol intermediate. The active site of the structure of DHQase in complex with the transition state analog also includes molecules of tartrate and glycerol, which provide a basis for further inhibitor design.
About this Structure
1GU1 is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor., Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ, Structure. 2002 Apr;10(4):493-503. PMID:11937054
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