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< | ==Crystal structure of Helicobacter pylori Undecaprenyl Pyrophosphate Synthase== | ||
<StructureSection load='2d2r' size='340' side='right'caption='[[2d2r]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2d2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2R 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]] 1.88Å</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=2d2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2r OCA], [https://pdbe.org/2d2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d2r RCSB], [https://www.ebi.ac.uk/pdbsum/2d2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d2r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ISPT_HELPY ISPT_HELPY] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | |||
== 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/d2/2d2r_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=2d2r ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Helicobacter pylori colonizes the human gastric epithelium and causes diseases such as gastritis, peptic ulcers, and stomach cancer. Undecaprenyl pyrophosphate synthase (UPPS), which catalyzes consecutive condensation reactions of farnesyl pyrophosphate with eight isopentenyl pyrophosphate to form lipid carrier for bacterial peptidoglycan biosynthesis, represents a potential target for developing new antibiotics. In this study, we solved the crystal structure of H. pylori UPPS and performed virtual screening of inhibitors from a library of 58,635 compounds. Two hits were found to exhibit differential activities against Helicobacter pylori and Escherichia coli UPPS, giving the possibility of developing antibiotics specially targeting pathogenic H. pylori without killing the intestinal E. coli. | |||
Structure-based inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases.,Kuo CJ, Guo RT, Lu IL, Liu HG, Wu SY, Ko TP, Wang AH, Liang PH J Biomed Biotechnol. 2008;2008:841312. PMID:18382620<ref>PMID:18382620</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2d2r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Undecaprenyl pyrophosphate synthase|Undecaprenyl pyrophosphate synthase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Chen | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Chen CL]] | ||
[[Category: Cheng | [[Category: Cheng YL]] | ||
[[Category: Guo | [[Category: Cheng YS]] | ||
[[Category: Ko | [[Category: Guo RT]] | ||
[[Category: Kuo | [[Category: Ko TP]] | ||
[[Category: Liang | [[Category: Kuo CJ]] | ||
[[Category: Wang | [[Category: Liang PH]] | ||
[[Category: Wang AH-J]] | |||
Latest revision as of 11:23, 25 October 2023
Crystal structure of Helicobacter pylori Undecaprenyl Pyrophosphate SynthaseCrystal structure of Helicobacter pylori Undecaprenyl Pyrophosphate Synthase
Structural highlights
FunctionISPT_HELPY Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHelicobacter pylori colonizes the human gastric epithelium and causes diseases such as gastritis, peptic ulcers, and stomach cancer. Undecaprenyl pyrophosphate synthase (UPPS), which catalyzes consecutive condensation reactions of farnesyl pyrophosphate with eight isopentenyl pyrophosphate to form lipid carrier for bacterial peptidoglycan biosynthesis, represents a potential target for developing new antibiotics. In this study, we solved the crystal structure of H. pylori UPPS and performed virtual screening of inhibitors from a library of 58,635 compounds. Two hits were found to exhibit differential activities against Helicobacter pylori and Escherichia coli UPPS, giving the possibility of developing antibiotics specially targeting pathogenic H. pylori without killing the intestinal E. coli. Structure-based inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases.,Kuo CJ, Guo RT, Lu IL, Liu HG, Wu SY, Ko TP, Wang AH, Liang PH J Biomed Biotechnol. 2008;2008:841312. PMID:18382620[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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