1zuh: Difference between revisions

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-{{Seed}}
-[[Image:1zuh.png|left|200px]]
-<!--
+==Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase==
-The line below this paragraph, containing "STRUCTURE_1zuh", creates the "Structure Box" on the page.
+<StructureSection load='1zuh' size='340' side='right'caption='[[1zuh]], [[Resolution|resolution]] 1.80&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'>[[1zuh]] 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=1ZUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUH 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]] 1.8&#8491;</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=1zuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zuh OCA], [https://pdbe.org/1zuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zuh RCSB], [https://www.ebi.ac.uk/pdbsum/1zuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zuh ProSAT]</span></td></tr>
-{{STRUCTURE_1zuh|  PDB=1zuh  |  SCENE=  }}
+</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/1zuh_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=1zuh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase===
+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:16291688<ref>PMID:16291688</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1zuh" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16291688}}, adds the Publication Abstract to the page
+*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16291688 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16291688}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Helicobacter pylori 26695]]
-ZUH is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUH OCA].
+[[Category: Large Structures]]
+[[Category: Chang YN]]
-==Reference==
+[[Category: Cheng WC]]
-<ref group="xtra">PMID:16291688</ref><references group="xtra"/>
+[[Category: Wang WC]]
-[[Category: Helicobacter pylori]]
-[[Category: Shikimate kinase]]
-[[Category: Chang, Y N.]]
-[[Category: Cheng, W C.]]
-[[Category: Wang, W C.]]
-[[Category: Alpha-beta protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:48:06 2009''