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| | <StructureSection load='1nva' size='340' side='right'caption='[[1nva]], [[Resolution|resolution]] 2.62Å' scene=''> | | <StructureSection load='1nva' size='340' side='right'caption='[[1nva]], [[Resolution|resolution]] 2.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nva]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._nidulans A. nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nva]] 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=1NVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NVA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.62Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nr5|1nr5]], [[1nrx|1nrx]], [[1nve|1nve]], [[1nvd|1nvd]], [[1nvb|1nvb]], [[1nua|1nua]], [[1nvf|1nvf]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AROMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 A. nidulans])</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=1nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nva OCA], [https://pdbe.org/1nva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nva RCSB], [https://www.ebi.ac.uk/pdbsum/1nva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nva ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_synthase 3-dehydroquinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.4 4.2.3.4] </span></td></tr> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nva OCA], [http://pdbe.org/1nva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nva RCSB], [http://www.ebi.ac.uk/pdbsum/1nva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nva ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-dehydroquinate synthase]] | + | [[Category: Aspergillus nidulans]] |
| - | [[Category: A. nidulans]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hawkins, A R]] | + | [[Category: Hawkins AR]] |
| - | [[Category: Lamb, H K]] | + | [[Category: Lamb HK]] |
| - | [[Category: Nichols, C E]] | + | [[Category: Nichols CE]] |
| - | [[Category: Ren, J]] | + | [[Category: Ren J]] |
| - | [[Category: Stammers, D K]] | + | [[Category: Stammers DK]] |
| - | [[Category: Aromatic amino acid biosynthesis]]
| + | |
| - | [[Category: Cyclase]]
| + | |
| - | [[Category: Dhq]]
| + | |
| - | [[Category: Domain movement]]
| + | |
| - | [[Category: Form d]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Open form]]
| + | |
| - | [[Category: Shikimate pathway]]
| + | |
| Structural highlights
Function
ARO1_EMENI The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.[HAMAP-Rule:MF_03143]
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 PubMed
In order to investigate systematically substrate and cofactor-induced conformational changes in the enzyme dehydroquinate synthase (DHQS), eight structures representing a series of differently liganded states have been determined in a total of six crystal forms. DHQS in the absence of the substrate analogue carbaphosphonate, either unliganded or in the presence of NAD or ADP, is in an open form where a relative rotation of 11-13 degrees between N and C-terminal domains occurs.Analysis of torsion angle difference plots between sets of structures reveals eight rearrangements that appear relevant to domain closure and a further six related to crystal packing. Overlapping 21 different copies of the individual N and C-terminal DHQS domains further reveals a series of pivot points about which these movements occur and illustrates the way in which widely separated secondary structure elements are mechanically inter-linked to form "composite elements", which propagate structural changes across large distances.This analysis has provided insight into the basis of DHQS ligand-initiated domain closure and gives rise to the proposal of an ordered sequence of events involving substrate binding, and local rearrangements within the active site that are propagated to the hinge regions, leading to closure of the active-site cleft.
Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase.,Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:12614613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK. Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase. J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:12614613
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