1gu1

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[[Image:1gu1.gif|left|200px]]<br /><applet load="1gu1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gu1.gif|left|200px]]
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caption="1gu1, resolution 1.80&Aring;" />
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'''CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH 2,3-ANYDRO-QUINIC ACID'''<br />
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{{Structure
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|PDB= 1gu1 |SIZE=350|CAPTION= <scene name='initialview01'>1gu1</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=FAA:Fa1+Binding+Site+For+Chain+L'>FAA</scene>
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|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> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR COMPLEXED WITH 2,3-ANYDRO-QUINIC ACID'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GU1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=FA1:'>FA1</scene>, <scene name='pdbligand=TLA:'>TLA</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=FAA:Fa1+Binding+Site+For+Chain+L'>FAA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU1 OCA].
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1GU1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11937054 11937054]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11937054 11937054]
[[Category: 3-dehydroquinate dehydratase]]
[[Category: 3-dehydroquinate dehydratase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: type ii dehydroquinase]]
[[Category: type ii dehydroquinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:56 2008''

Revision as of 09:27, 20 March 2008

Image:1gu1.gif


PDB ID 1gu1

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: , , and
Activity: 3-dehydroquinate dehydratase, with EC number 4.2.1.10
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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