5g48
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==H.pylori Beta clamp in complex with Diflunisal== | |
| + | <StructureSection load='5g48' size='340' side='right' caption='[[5g48]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5g48]] is a 2 chain structure with 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=5G48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G48 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1FL:5-(2,4-DIFLUOROPHENYL)-2-HYDROXY-BENZOIC+ACID'>1FL</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g48 OCA], [http://pdbe.org/5g48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g48 RCSB], [http://www.ebi.ac.uk/pdbsum/5g48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g48 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DPO3B_HELPY DPO3B_HELPY]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The beta-clamp is the processivity-promoting factor for most of the enzymes in prokaryotic DNA replication; hence, it is a crucial drug target. In the present study, we investigated the beta-clamp from Helicobacter pylori, aiming to seek potential drug molecules against this gastric-cancer-causing bacterium. An in silico screening of Food and Drug Administration (FDA) approved drugs against the H. pylori beta-clamp, followed by its in vitro inhibition using a surface competition approach, yielded the drug diflunisal as a positive initial hit. Diflunisal inhibits the growth of H. pylori in the micromolar range. We determined the structure of diflunisal in complex with the beta-clamp to show that the drug binds at subsite I, which is a protein-protein interaction site. Successful identification of FDA-approved molecules against H. pylori may lead to better and faster drug development. | ||
| - | + | Targeting the beta-clamp in Helicobacter pylori with FDA-approved drugs reveals micromolar inhibition by diflunisal.,Pandey P, Verma V, Gautam G, Kumari N, Dhar SK, Gourinath S FEBS Lett. 2017 Aug;591(15):2311-2322. doi: 10.1002/1873-3468.12734. Epub 2017, Jul 26. PMID:28656718<ref>PMID:28656718</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5g48" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
[[Category: Gourinath, S]] | [[Category: Gourinath, S]] | ||
| + | [[Category: Pandey, P]] | ||
| + | [[Category: Dna sliding clamp]] | ||
| + | [[Category: Processivity promoting factor]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:05, 17 August 2017
H.pylori Beta clamp in complex with Diflunisal
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