1gu0: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1gu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gu0, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| (16 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR== | ||
The structure of the type II DHQase from Streptomyces coelicolor has been | <StructureSection load='1gu0' size='340' side='right'caption='[[1gu0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gu0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GU0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gu0 OCA], [https://pdbe.org/1gu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gu0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AROQ_STRCO AROQ_STRCO] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1gu0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gu0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:11937054</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 1gu0" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
[[Category: Coggins | [[Category: Coggins JR]] | ||
[[Category: Hunter | [[Category: Hunter IS]] | ||
[[Category: Krell | [[Category: Krell T]] | ||
[[Category: Lapthorn | [[Category: Lapthorn AJ]] | ||
[[Category: Robinson | [[Category: Robinson D]] | ||
[[Category: Roszak | [[Category: Roszak AW]] | ||
Latest revision as of 15:06, 13 December 2023
CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLORCRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM STREPTOMYCES COELICOLOR
Structural highlights
FunctionAROQ_STRCO Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||