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==Structural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase== | ==Structural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase== | ||
<StructureSection load='3h2a' size='340' side='right' caption='[[3h2a]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3h2a' size='340' side='right' caption='[[3h2a]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3h2a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3h2a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis_a2012 Bacillus anthracis a2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H2A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B57:2,6-DIAMINO-5-NITROPYRIMIDIN-4(3H)-ONE'>B57</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B57:2,6-DIAMINO-5-NITROPYRIMIDIN-4(3H)-ONE'>B57</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tww|1tww]], [[1twz|1twz]], [[1tx0|1tx0]], [[1tx2|1tx2]], [[1tws|1tws]], [[3h21|3h21]], [[3h22|3h22]], [[3h23|3h23]], [[3h24|3h24]], [[3h26|3h26]], [[3h2c|3h2c]], [[3h2e|3h2e]], [[3h2f|3h2f]], [[3h2m|3h2m]], [[3h2n|3h2n]], [[3h2o|3h2o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tww|1tww]], [[1twz|1twz]], [[1tx0|1tx0]], [[1tx2|1tx2]], [[1tws|1tws]], [[3h21|3h21]], [[3h22|3h22]], [[3h23|3h23]], [[3h24|3h24]], [[3h26|3h26]], [[3h2c|3h2c]], [[3h2e|3h2e]], [[3h2f|3h2f]], [[3h2m|3h2m]], [[3h2n|3h2n]], [[3h2o|3h2o]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, BAO_0074 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=191218 Bacillus anthracis | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, BAO_0074 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=191218 Bacillus anthracis A2012])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] </span></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=3h2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h2a RCSB], [http://www.ebi.ac.uk/pdbsum/3h2a PDBsum]</span></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=3h2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h2a OCA], [http://pdbe.org/3h2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h2a RCSB], [http://www.ebi.ac.uk/pdbsum/3h2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h2a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=3h2a ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3h2a" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus anthracis | [[Category: Bacillus anthracis a2012]] | ||
[[Category: Dihydropteroate synthase]] | [[Category: Dihydropteroate synthase]] | ||
[[Category: White, S W]] | [[Category: White, S W]] | ||
Revision as of 20:43, 11 August 2016
Structural Studies of Pterin-Based Inhibitors of Dihydropteroate SynthaseStructural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase
Structural highlights
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 PubMedDihydropteroate synthase (DHPS) is a key enzyme in bacterial folate synthesis and the target of the sulfonamide class of antibacterials. Resistance and toxicities associated with sulfonamides have led to a decrease in their clinical use. Compounds that bind to the pterin binding site of DHPS, as opposed to the p-amino benzoic acid (pABA) binding site targeted by the sulfonamide agents, are anticipated to bypass sulfonamide resistance. To identify such inhibitors and map the pterin binding pocket, we have performed virtual screening, synthetic, and structural studies using Bacillus anthracis DHPS. Several compounds with inhibitory activity have been identified, and crystal structures have been determined that show how the compounds engage the pterin site. The structural studies identify the key binding elements and have been used to generate a structure-activity based pharmacophore map that will facilitate the development of the next generation of DHPS inhibitors which specifically target the pterin site. Structural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase.,Hevener KE, Yun MK, Qi J, Kerr ID, Babaoglu K, Hurdle JG, Balakrishna K, White SW, Lee RE J Med Chem. 2009 Nov 9. PMID:19899766[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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