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==Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor== | ==Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor== | ||
<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 with sequence from [ | <table><tr><td colspan='2'>[[4b4w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ATCC_19606_=_CIP_70.34_=_JCM_6841 Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841]. 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><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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='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 == | |||
[https://www.uniprot.org/uniprot/D0CBC8_ACIB2 D0CBC8_ACIB2] 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] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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 4b4w" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acinetobacter baumannii | [[Category: Acinetobacter baumannii ATCC 19606 = CIP 70 34 = JCM 6841]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Eadsforth TC]] | ||
[[Category: | [[Category: Hunter WN]] | ||
[[Category: | [[Category: Maluf FV]] | ||
Latest revision as of 14:43, 20 December 2023
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
FunctionD0CBC8_ACIB2 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] 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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