1zui: Difference between revisions

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OCA

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-[[Image:1zui.gif|left|200px]]<br /><applet load="1zui" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1zui, resolution 2.300&Aring;" />
-'''Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase'''<br />
-==Overview==
+==Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase==
-Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of, the 3-hydroxyl group of shikimic acid in the presence of ATP. As the fifth, key step in the shikimate pathway for aromatic amino acid biosynthesis in, bacteria, fungi, and plants, but not mammals, shikimate kinase represents, an attractive target for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here, we report the 1.8-Angstroms, crystal structure of Helicobacter pylori shikimate kinase (HpSK). The, crystal structure shows a three-layer alpha/beta fold consisting of a, central sheet of five parallel beta-strands flanked by seven, alpha-helices. An HpSK-shikimate-PO(4) complex was also determined and, refined to 2.3 Angstroms, revealing induced-fit movement from an open to a, closed form on substrate binding. Shikimate is located above a short 3(10), helix formed by a strictly conserved motif (GGGXV) after beta(3)., Moreover, several highly conserved charged residues including Asp33 (in a, conserved DT/SD motif), Arg57, and Arg132 (interacting with shikimate) are, identified, guiding the development of novel inhibitors of shikimate, kinase.
+<StructureSection load='1zui' size='340' side='right'caption='[[1zui]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1zui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUI 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]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</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=1zui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zui OCA], [https://pdbe.org/1zui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zui RCSB], [https://www.ebi.ac.uk/pdbsum/1zui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zui ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AROK_HELPY AROK_HELPY] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:16291688</ref>
+== 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/zu/1zui_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=1zui ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-ZUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with PO4 and SKM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZUI OCA].
+*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase., Cheng WC, Chang YN, Wang WC, J Bacteriol. 2005 Dec;187(23):8156-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16291688 16291688]
+__TOC__
-[[Category: Helicobacter pylori]]
+</StructureSection>
-[[Category: Shikimate kinase]]
+[[Category: Helicobacter pylori 26695]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Chang, Y.N.]]
+[[Category: Chang YN]]
-[[Category: Cheng, W.C.]]
+[[Category: Cheng WC]]
-[[Category: Wang, W.C.]]
+[[Category: Wang WC]]
-[[Category: PO4]]
-[[Category: SKM]]
-[[Category: alpha-beta protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:40:14 2007''