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4b4u

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[[Image:4b4u.png|left|200px]]
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==Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor==
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<StructureSection load='4b4u' size='340' side='right' caption='[[4b4u]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b4v|4b4v]], [[4b4w|4b4w]]</td></tr>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_4b4u| PDB=4b4u | SCENE= }}
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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>
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===Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor===
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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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{{ABSTRACT_PUBMED_23050773}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[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].
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</StructureSection>
[[Category: Acinetobacter baumannii atcc 19606 = cip 70 34]]
[[Category: Acinetobacter baumannii atcc 19606 = cip 70 34]]
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[[Category: Eadsforth, T C.]]
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[[Category: Eadsforth, T C]]
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[[Category: Hunter, W N.]]
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[[Category: Hunter, W N]]
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[[Category: Maluf, F V.]]
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[[Category: Maluf, F V]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 16:36, 9 December 2014

Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor

4b4u, resolution 1.45Å

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