1nhg: Difference between revisions

Revision as of 14:59, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nhg.png

Template:STRUCTURE 1nhg

CRYSTAL STRUCTURE ANALYSIS OF PLASMODIUM FALCIPARUM ENOYL-ACYL-CARRIER-PROTEIN REDUCTASE WITH TRICLOSANCRYSTAL STRUCTURE ANALYSIS OF PLASMODIUM FALCIPARUM ENOYL-ACYL-CARRIER-PROTEIN REDUCTASE WITH TRICLOSAN

Template:ABSTRACT PUBMED 11792710

About this StructureAbout this Structure

1NHG is a Protein complex structure of sequences from Plasmodium falciparum. Full crystallographic information is available from OCA.

ReferenceReference

Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase., Perozzo R, Kuo M, Sidhu AS, Valiyaveettil JT, Bittman R, Jacobs WR Jr, Fidock DA, Sacchettini JC, J Biol Chem. 2002 Apr 12;277(15):13106-14. Epub 2002 Jan 15. PMID:11792710

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OCA

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 {{STRUCTURE_1nhg|  PDB=1nhg  |  SCENE=  }}
-'''CRYSTAL STRUCTURE ANALYSIS OF PLASMODIUM FALCIPARUM ENOYL-ACYL-CARRIER-PROTEIN REDUCTASE WITH TRICLOSAN'''
+===CRYSTAL STRUCTURE ANALYSIS OF PLASMODIUM FALCIPARUM ENOYL-ACYL-CARRIER-PROTEIN REDUCTASE WITH TRICLOSAN===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11792710}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11792710 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11792710}}
 ==About this Structure==
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 [[Category: Rossmann fold]]
 [[Category: Short chain dehydrogenase reductase]]
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