2c07

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(New page: 200px<br /> <applet load="2c07" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c07, resolution 1.50&Aring;" /> '''OXOACYL-ACP REDUCTA...)
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==About this Structure==
==About this Structure==
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2C07 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C07 OCA]].
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2C07 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C07 OCA]].
==Reference==
==Reference==
Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis., Wickramasinghe SR, Inglis KA, Urch JE, Muller S, van Aalten DM, Fairlamb AH, Biochem J. 2006 Jan 15;393(Pt 2):447-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16225460 16225460]
Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis., Wickramasinghe SR, Inglis KA, Urch JE, Muller S, van Aalten DM, Fairlamb AH, Biochem J. 2006 Jan 15;393(Pt 2):447-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16225460 16225460]
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[[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: short-chain alcohol reductase]]
[[Category: short-chain alcohol reductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:48:41 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:49:49 2007''

Revision as of 10:45, 30 October 2007


2c07, resolution 1.50Å

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OXOACYL-ACP REDUCTASE OF PLASMODIUM FALCIPARUM

Overview

Type II fatty acid biosynthesis represents an attractive target for the, discovery of new antimalarial drugs. Previous studies have identified, malarial ENR (enoyl acyl-carrier-protein reductase, or FabI) as the target, for the antiseptic triclosan. In the present paper, we report the, biochemical properties and 1.5 A (1 A=0.1 nm) crystal structure of OAR, (3-oxoacyl acyl-carrier-protein reductase, or FabG), the second reductive, step in fatty acid biosynthesis and its inhibition by hexachlorophene., Under optimal conditions of pH and ionic strength, Plasmodium falciparum, OAR displays kinetic properties similar to those of OAR from bacteria or, plants. Activity with NADH is <3% of that with NADPH. Fluorescence, enhancement studies indicate that NADPH can bind to the free enzyme, ... [(full description)]

About this Structure

2C07 is a [Single protein] structure of sequence from [Plasmodium falciparum] with SO4 as [ligand]. Active as [[acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase]], with EC number [1.1.1.100]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis., Wickramasinghe SR, Inglis KA, Urch JE, Muller S, van Aalten DM, Fairlamb AH, Biochem J. 2006 Jan 15;393(Pt 2):447-57. PMID:16225460 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]

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