2o2s: Difference between revisions

Revision as of 03:06, 29 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:2o2s.png

Template:STRUCTURE 2o2s

The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosanThe structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan

Template:ABSTRACT PUBMED 17327670

About this StructureAbout this Structure

2O2S is a Single protein structure of sequence from Toxoplasma gondii. Full crystallographic information is available from OCA.

ReferenceReference

Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents., Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):328-38. Epub 2007, Feb 21. PMID:17327670

Expression, purification and preliminary crystallographic analysis of the Toxoplasma gondii enoyl reductase., Muench SP, Prigge ST, Zhu L, Kirisits MJ, Roberts CW, Wernimont S, McLeod R, Rice DW, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):604-6. Epub 2006 May 31. PMID:16754994

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2o2s|  PDB=2o2s  |  SCENE=  }}
-'''The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan'''
+===The structure of T. gondii enoyl acyl carrier protein reductase in complex with NAD and triclosan===
-==Overview==
+<!--
-Recent studies have demonstrated that submicromolar concentrations of the biocide triclosan arrest the growth of the apicomplexan parasites Plasmodium falciparum and Toxoplasma gondii and inhibit the activity of the apicomplexan enoyl acyl carrier protein reductase (ENR). The crystal structures of T. gondii and P. falciparum ENR in complex with NAD(+) and triclosan and of T. gondii ENR in an apo form have been solved to 2.6, 2.2 and 2.8 A, respectively. The structures of T. gondii ENR have revealed that, as in its bacterial and plant homologues, a loop region which flanks the active site becomes ordered upon inhibitor binding, resulting in the slow tight binding of triclosan. In addition, the T. gondii ENR-triclosan complex reveals the folding of a hydrophilic insert common to the apicomplexan family that flanks the substrate-binding domain and is disordered in all other reported apicomplexan ENR structures. Structural comparison of the apicomplexan ENR structures with their bacterial and plant counterparts has revealed that although the active sites of the parasite enzymes are broadly similar to those of their bacterial counterparts, there are a number of important differences within the drug-binding pocket that reduce the packing interactions formed with several inhibitors in the apicomplexan ENR enzymes. Together with other significant structural differences, this provides a possible explanation of the lower affinity of the parasite ENR enzyme family for aminopyridine-based inhibitors, suggesting that an effective antiparasitic agent may well be distinct from equivalent antimicrobials.
+The line below this paragraph, {{ABSTRACT_PUBMED_17327670}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17327670 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17327670}}
 ==About this Structure==
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 ==Reference==
 Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents., Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):328-38. Epub 2007, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17327670 17327670]
+Expression, purification and preliminary crystallographic analysis of the Toxoplasma gondii enoyl reductase., Muench SP, Prigge ST, Zhu L, Kirisits MJ, Roberts CW, Wernimont S, McLeod R, Rice DW, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):604-6. Epub 2006 May 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16754994 16754994]
 [[Category: Single protein]]
 [[Category: Toxoplasma gondii]]
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 [[Category: Rossmann fold]]
 [[Category: Triclosan]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:06:17 2008''