1nrx: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1nrx.png|left|200px]]
-<!--
+==Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ and NAD==
-The line below this paragraph, containing "STRUCTURE_1nrx", creates the "Structure Box" on the page.
+<StructureSection load='1nrx' size='340' side='right'caption='[[1nrx]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1nrx]] 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=1NRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NRX FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1nrx|  PDB=1nrx  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nrx OCA], [https://pdbe.org/1nrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nrx RCSB], [https://www.ebi.ac.uk/pdbsum/1nrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nrx 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/nr/1nrx_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=1nrx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+ and NAD===
+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<ref>PMID:12614613</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12614613}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1nrx" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12614613 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12614613}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Aspergillus nidulans]]
-NRX is a 2 chains structure of sequences 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=1NRX OCA].
+[[Category: Large Structures]]
+[[Category: Hawkins AR]]
-==Reference==
+[[Category: Lamb HK]]
-<ref group="xtra">PMID:12614613</ref><references group="xtra"/>
+[[Category: Nichols CE]]
-[[Category: 3-dehydroquinate synthase]]
+[[Category: Ren J]]
-[[Category: Emericella nidulans]]
+[[Category: Stammers DK]]
-[[Category: Hawkins, A R.]]
-[[Category: Lamb, H K.]]
-[[Category: Nichols, C E.]]
-[[Category: Ren, J.]]
-[[Category: Stammers, D K.]]
-[[Category: Aromatic amino acid biosynthesis]]
-[[Category: Closed form]]
-[[Category: Cyclase]]
-[[Category: Dhq]]
-[[Category: Domain movement]]
-[[Category: Form f]]
-[[Category: Lyase]]
-[[Category: Shikimate pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:55:09 2009''