3juk

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{{Seed}}
 
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[[Image:3juk.png|left|200px]]
 
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==The Crystal Structure of UDP-glucose pyrophosphorylase complexed with UDP-glucose==
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The line below this paragraph, containing "STRUCTURE_3juk", creates the "Structure Box" on the page.
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<StructureSection load='3juk' size='340' side='right'caption='[[3juk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3juk]] is a 4 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=3JUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JUK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
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{{STRUCTURE_3juk| PDB=3juk | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3juk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3juk OCA], [https://pdbe.org/3juk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3juk RCSB], [https://www.ebi.ac.uk/pdbsum/3juk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3juk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O25363_HELPY O25363_HELPY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/3juk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3juk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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UDP-glucose pyrophosphorylases (UGPase; EC 2.7.7.9) catalyze the conversion of UTP and glucose-1-phosphate to UDP-glucose and pyrophosphate and vice versa. Prokaryotic UGPases are distinct from their eukaryotic counterparts and are considered appropriate targets for the development of novel antibacterial agents since their product, UDP-glucose, is indispensable for the biosynthesis of virulence factors such as lipopolysaccharides and capsular polysaccharides. In this study, the crystal structures of UGPase from Helicobacter pylori (HpUGPase) were determined in apo- and UDP-glucose/Mg(2+)-bound forms at 2.9 A and 2.3 A resolutions, respectively. HpUGPase is a homotetramer and its active site is located in a deep pocket of each subunit. Magnesium ion is coordinated by Asp130, two oxygen atoms of phosphoryl groups, and three water molecules with octahedral geometry. Isothermal titration calorimetry analyses demonstrated that Mg(2+) ion plays a key role in the enzymatic activity of UGPase by enhancing the binding of UGPase to UTP or UDP-glucose, suggesting that this reaction is catalyzed by an ordered sequential Bi Bi mechanism. Furthermore, the crystal structure explains the specificity for uracil bases. The current structural study combined with functional analyses provides essential information for understanding the reaction mechanism of bacterial UGPases, as well as a platform for the development of novel antibacterial agents.
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===The Crystal Structure of UDP-glucose pyrophosphorylase complexed with UDP-glucose===
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Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase.,Kim H, Choi J, Kim T, Lokanath NK, Ha SC, Suh SW, Hwang HY, Kim KK Mol Cells. 2010 Mar 15. PMID:20238176<ref>PMID:20238176</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20238176}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3juk" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20238176 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20238176}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Helicobacter pylori 26695]]
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3JUK is a 4 chains structure with sequences 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=3JUK OCA].
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[[Category: Large Structures]]
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[[Category: Kim H]]
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==Reference==
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[[Category: Kim KK]]
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<ref group="xtra">PMID:20238176</ref><references group="xtra"/>
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[[Category: Helicobacter pylori]]
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[[Category: UTP--glucose-1-phosphate uridylyltransferase]]
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[[Category: Kim, H.]]
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[[Category: Kim, K K.]]
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[[Category: Helicobacter pylori]]
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[[Category: Transferase]]
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[[Category: Udp-glucose pyrophosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:02:31 2010''
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Current revision

The Crystal Structure of UDP-glucose pyrophosphorylase complexed with UDP-glucose

PDB ID 3juk

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