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{{STRUCTURE_1sg6|  PDB=1sg6  |  SCENE=  }}
===Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D===
{{ABSTRACT_PUBMED_15103156}}


==Function==
==Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D==
[[http://www.uniprot.org/uniprot/ARO1_EMENI ARO1_EMENI]] The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.[HAMAP-Rule:MF_03143]  
<StructureSection load='1sg6' size='340' side='right'caption='[[1sg6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sg6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SG6 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1sg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg6 OCA], [https://pdbe.org/1sg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sg6 RCSB], [https://www.ebi.ac.uk/pdbsum/1sg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARO1_EMENI ARO1_EMENI] The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.[HAMAP-Rule:MF_03143]
== 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/sg/1sg6_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=1sg6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystallization of Aspergillus nidulans 3-dehydroquinate synthase (DHQS), following turnover of the enzyme by addition of the substrate DAHP, gave a new crystal form (form J). Although the crystals have dimensions of only 50 x 20 x 5 micro m, they are well ordered, diffracting to 1.7 A. The space group is C222(1), with unit-cell parameters a = 90.0, b = 103.7, c = 177.4 A. Structure determination and refinement to R = 0.19 (R(free) = 0.25) shows the DHQS is in the 'open' form with the substrate site unoccupied but with some loop regions perturbed. Previous crystals of open-form DHQS only diffracted to 2.5 A resolution. The use of enzyme turnover may be applicable in other systems in attempts to improve crystal quality.


==About this Structure==
Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.,Nichols CE, Hawkins AR, Stammers DK Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:15103156<ref>PMID:15103156</ref>
[[1sg6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SG6 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:015103156</ref><references group="xtra"/><references/>
</div>
[[Category: 3-dehydroquinate synthase]]
<div class="pdbe-citations 1sg6" style="background-color:#fffaf0;"></div>
[[Category: Emericella nidulans]]
== References ==
[[Category: Hawkins, A R.]]
<references/>
[[Category: Nichols, C E.]]
__TOC__
[[Category: Stammers, D K.]]
</StructureSection>
[[Category: Aromatic amino acid biosynthesis]]
[[Category: Aspergillus nidulans]]
[[Category: Cyclase]]
[[Category: Large Structures]]
[[Category: Dhq]]
[[Category: Hawkins AR]]
[[Category: Domain movement]]
[[Category: Nichols CE]]
[[Category: Form j]]
[[Category: Stammers DK]]
[[Category: Lyase]]
[[Category: Open form]]
[[Category: Shikimate pathway]]
Retrieved from "https://proteopedia.org/1sg6"