4b4u: Difference between revisions
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[[ | ==Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor== | ||
<StructureSection load='4b4u' size='340' side='right' caption='[[4b4u]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b4u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii_atcc_19606_=_cip_70.34 Acinetobacter baumannii atcc 19606 = cip 70.34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B4U FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b4v|4b4v]], [[4b4w|4b4w]]</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=4b4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b4u RCSB], [http://www.ebi.ac.uk/pdbsum/4b4u PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:23050773</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Acinetobacter baumannii atcc 19606 = cip 70 34]] | [[Category: Acinetobacter baumannii atcc 19606 = cip 70 34]] | ||
[[Category: Eadsforth, T C | [[Category: Eadsforth, T C]] | ||
[[Category: Hunter, W N | [[Category: Hunter, W N]] | ||
[[Category: Maluf, F V | [[Category: Maluf, F V]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
