1xal: Difference between revisions

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-[[Image:1xal.gif|left|200px]]<br /><applet load="1xal" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1xal, resolution 2.80&Aring;" />
-'''CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE (SOAK)'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE (SOAK)==
-Dehydroquinate synthase (DHQS) is a potential target for the development, of novel broad-spectrum antimicrobial drugs, active against both, prokaryotes and lower eukaryotes. Structures have been reported for, Aspergillus nidulans DHQS (AnDHQS) in complexes with a range of ligands., Analysis of these AnDHQS structures showed that a large-scale domain, movement occurs during the normal catalytic cycle, with a complex series, of structural elements propagating substrate binding-induced, conformational changes away from the active site to distal locations., Compared to corresponding fungal enzymes, DHQS from bacterial species are, both mono-functional and significantly smaller. We have therefore, determined the structure of Staphylococcus aureus DHQS (SaDHQS) in five, liganded states, allowing comparison of ligand-induced conformational, changes and mechanisms of domain closure between fungal and bacterial, enzymes. This comparative analysis shows that substrate binding initiates, a large-scale domain closure in both species' DHQS and that the active, site stereochemistry, of the catalytically competent closed-form enzyme, thus produced, is also highly conserved. However, comparison of AnDHQS and, SaDHQS open-form structures, and analysis of the putative dynamic, processes by which the transition to the closed-form states are made, shows a far lower degree of similarity, indicating a significant, structural divergence. As a result, both the nature of the propagation of, conformational change and the mechanical systems involved in this, propagation are quite different between the DHQSs from the two species.
+<StructureSection load='1xal' size='340' side='right'caption='[[1xal]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1xal]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XAL FirstGlance]. <br>
-XAL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with ZN, NAD and CRB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XAL OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRB:[1R-(1ALPHA,3BETA,4ALPHA,5BETA)]-5-(PHOSPHONOMETHYL)-1,3,4-TRIHYDROXYCYCLOHEXANE-1-CARBOXYLIC+ACID'>CRB</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xal OCA], [https://pdbe.org/1xal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xal RCSB], [https://www.ebi.ac.uk/pdbsum/1xal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xal ProSAT]</span></td></tr>
-Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases., Nichols CE, Ren J, Leslie K, Dhaliwal B, Lockyer M, Charles I, Hawkins AR, Stammers DK, J Mol Biol. 2004 Oct 22;343(3):533-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15465043 15465043]
+</table>
-[[Category: 3-dehydroquinate synthase]]
+== Function ==
-[[Category: Single protein]]
+[https://www.uniprot.org/uniprot/AROB_STAAR AROB_STAAR]
+== 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/xa/1xal_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=1xal ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Staphylococcus aureus]]
-[[Category: Charles, I.]]
+[[Category: Charles I]]
-[[Category: Dhaliwal, B.]]
+[[Category: Dhaliwal B]]
-[[Category: Hawkins, A.R.]]
+[[Category: Hawkins AR]]
-[[Category: Leslie, K.]]
+[[Category: Leslie K]]
-[[Category: Lockyer, M.]]
+[[Category: Lockyer M]]
-[[Category: Nichols, C.E.]]
+[[Category: Nichols CE]]
-[[Category: Ren, J.]]
+[[Category: Ren J]]
-[[Category: Stammers, D.K.]]
+[[Category: Stammers DK]]
-[[Category: CRB]]
-[[Category: NAD]]
-[[Category: ZN]]
-[[Category: aromatic amino acid biosynthesis]]
-[[Category: closed form]]
-[[Category: cyclase]]
-[[Category: dhqs]]
-[[Category: domain movement]]
-[[Category: form b]]
-[[Category: lyase]]
-[[Category: sadhqs]]
-[[Category: shikimate pathway]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:56:52 2007''