4b4w: Difference between revisions
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<StructureSection load='4b4w' size='340' side='right'caption='[[4b4w]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4b4w' size='340' side='right'caption='[[4b4w]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b4w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4W OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4b4w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4W FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9L9:(2S)-2-[[4-[[2,4-BIS(AZANYL)-6-OXIDANYLIDENE-1H-PYRIMIDIN-5-YL]CARBAMOYLAMINO]PHENYL]CARBONYLAMINO]PENTANEDIOIC+ACID'>9L9</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9L9:(2S)-2-[[4-[[2,4-BIS(AZANYL)-6-OXIDANYLIDENE-1H-PYRIMIDIN-5-YL]CARBAMOYLAMINO]PHENYL]CARBONYLAMINO]PENTANEDIOIC+ACID'>9L9</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b4u|4b4u]], [[4b4v|4b4v]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b4u|4b4u]], [[4b4v|4b4v]]</div></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=4b4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4w OCA], [https://pdbe.org/4b4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4w RCSB], [https://www.ebi.ac.uk/pdbsum/4b4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/D0CBC8_ACIBA D0CBC8_ACIBA]] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.[HAMAP-Rule:MF_01576][SAAS:SAAS00020424] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 09:59, 31 August 2022
Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitorCrystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor
Structural highlights
Function[D0CBC8_ACIBA] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.[HAMAP-Rule:MF_01576][SAAS:SAAS00020424] Publication Abstract from PubMedThe bifunctional N(5) , N(10) methylenetetrahydrofolate dehydrogenase/cyclohydrolase (DHCH or FolD), widely distributed in prokaryotes and eukaryotes, is involved in biosynthesis of folate cofactors essential for growth and cellular development. The enzyme activities represent a potential antimicrobial drug target. We have characterized the kinetic properties of FolD from the Gram-negative pathogen Acinetobacter baumanni and determined high-resolution crystal structures of complexes with cofactor and two potent inhibitors. The data reveal new details with respect to the molecular basis of catalysis and potent inhibition. A major surprise was that our crystallographic data revealed a different structure for LY374571, an inhibitor studied as an antifolate, that was previously published. The implications of this observation are discussed. (c) 2012 The Authors Journal compilation (c) 2012 FEBS. Acinetobacter baumannii FolD ligand complexes; potent inhibitors of folate metabolism and a re-evaluation of the LY374571 structure.,Eadsforth TC, Maluf FV, Hunter WN FEBS J. 2012 Oct 10. doi: 10.1111/febs.12025. PMID:23050773[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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