3tzn

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Current revision (10:16, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3tzn' size='340' side='right'caption='[[3tzn]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
<StructureSection load='3tzn' size='340' side='right'caption='[[3tzn]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tzn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TZN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tzn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TZN FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tyu|3tyu]], [[3tzf|3tzf]], [[3tyz|3tyz]]</div></td></tr>
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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]] 2.083&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhpS, folP, y0683, YPO3501, YP_0582 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</td></tr>
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<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>
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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=3tzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tzn OCA], [https://pdbe.org/3tzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tzn RCSB], [https://www.ebi.ac.uk/pdbsum/3tzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tzn ProSAT]</span></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=3tzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tzn OCA], [https://pdbe.org/3tzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tzn RCSB], [https://www.ebi.ac.uk/pdbsum/3tzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tzn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q7CKJ1_YERPE Q7CKJ1_YERPE]] DHPS catalyzes the formation of the immediate precursor of folic acid.[RuleBase:RU361205]
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[https://www.uniprot.org/uniprot/A0A2S9PLG4_YERPE A0A2S9PLG4_YERPE] Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.[RuleBase:RU361205]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 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.
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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<ref>PMID:22383850</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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<div class="pdbe-citations 3tzn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dihydropteroate synthase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Wu, Y]]
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[[Category: Yersinia pestis]]
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[[Category: Tim barrel]]
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[[Category: Wu Y]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of the Yersinia pestis Dihydropteroate synthase.

PDB ID 3tzn

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