3tyd: Difference between revisions
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==Dihydropteroate Synthase in complex with PPi and DHP+== | ==Dihydropteroate Synthase in complex with PPi and DHP+== | ||
<StructureSection load='3tyd' size='340' side='right' caption='[[3tyd]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3tyd' size='340' side='right'caption='[[3tyd]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tyd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tyd]] is a 2 chain structure with sequence from [https://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=3TYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XHP:2-AMINO-6-METHYLIDENE-6,7-DIHYDROPTERIDIN-4(3H)-ONE'>XHP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XHP:2-AMINO-6-METHYLIDENE-6,7-DIHYDROPTERIDIN-4(3H)-ONE'>XHP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tws|1tws]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tws|1tws]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, BAS0071, BA_0071, GBAA_0071 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, BAS0071, BA_0071, GBAA_0071 ([https://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'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tyd OCA], [https://pdbe.org/3tyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tyd RCSB], [https://www.ebi.ac.uk/pdbsum/3tyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tyd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Dihydropteroate synthase|Dihydropteroate synthase]] | *[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 28: | ||
[[Category: Bacillus anthracis a2012]] | [[Category: Bacillus anthracis a2012]] | ||
[[Category: Dihydropteroate synthase]] | [[Category: Dihydropteroate synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: White, S W]] | [[Category: White, S W]] | ||
[[Category: Yun, M K]] | [[Category: Yun, M K]] | ||
Revision as of 08:50, 13 July 2022
Dihydropteroate Synthase in complex with PPi and DHP+Dihydropteroate Synthase in complex with PPi and DHP+
Structural highlights
Publication Abstract from PubMedThe sulfonamide antibiotics inhibit dihydropteroate synthase (DHPS), a key enzyme in the folate pathway of bacteria and primitive eukaryotes. However, resistance mutations have severely compromised the usefulness of these drugs. We report structural, computational, and mutagenesis studies on the catalytic and resistance mechanisms of DHPS. By performing the enzyme-catalyzed reaction in crystalline DHPS, we have structurally characterized key intermediates along the reaction pathway. Results support an S(N)1 reaction mechanism via formation of a novel cationic pterin intermediate. We also show that two conserved loops generate a substructure during catalysis that creates a specific binding pocket for p-aminobenzoic acid, one of the two DHPS substrates. This substructure, together with the pterin-binding pocket, explains the roles of the conserved active-site residues and reveals how sulfonamide resistance arises. Catalysis and sulfa drug resistance in dihydropteroate synthase.,Yun MK, Wu Y, Li Z, Zhao Y, Waddell MB, Ferreira AM, Lee RE, Bashford D, White SW Science. 2012 Mar 2;335(6072):1110-4. PMID:22383850[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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