1nhw

<StructureSection load='1nhw' size='340' side='right' caption='[[1nhw]], [[Resolution|resolution]] 2.35&Aring;' scene=''>

<table><tr><td colspan='2'>[[1nhw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NHW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCC:2-(2,4-DICHLORO-PHENYLAMINO)-PHENOL'>TCC</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nhd|1nhd]], [[1nhg|1nhg]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span></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=1nhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nhw OCA], [http://pdbe.org/1nhw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nhw RCSB], [http://www.ebi.ac.uk/pdbsum/1nhw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nhw ProSAT]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nh/1nhw_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The human malaria parasite Plasmodium falciparum synthesizes fatty acids using a type II pathway that is absent in humans. The final step in fatty acid elongation is catalyzed by enoyl acyl carrier protein reductase, a validated antimicrobial drug target. Here, we report the cloning and expression of the P. falciparum enoyl acyl carrier protein reductase gene, which encodes a 50-kDa protein (PfENR) predicted to target to the unique parasite apicoplast. Purified PfENR was crystallized, and its structure resolved as a binary complex with NADH, a ternary complex with triclosan and NAD(+), and as ternary complexes bound to the triclosan analogs 1 and 2 with NADH. Novel structural features were identified in the PfENR binding loop region that most closely resembled bacterial homologs; elsewhere the protein was similar to ENR from the plant Brassica napus (root mean square for Calphas, 0.30 A). Triclosan and its analogs 1 and 2 killed multidrug-resistant strains of intra-erythrocytic P. falciparum parasites at sub to low micromolar concentrations in vitro. These data define the structural basis of triclosan binding to PfENR and will facilitate structure-based optimization of PfENR inhibitors.

 

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== References ==

[[Category: Plafa]]

[[Category: Bittman, R]]

[[Category: Fidock, D A]]

[[Category: Jacobs, W R]]

[[Category: Kuo, M]]

[[Category: Perozzo, R]]

[[Category: Sacchettini, J C]]

[[Category: Sidhu, A S]]

[[Category: Valiyaveettil, J T]]

[[Category: Short chain dehydrogenase reductase]]