1uh5

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{{STRUCTURE_1uh5| PDB=1uh5 | SCENE= }}
{{STRUCTURE_1uh5| PDB=1uh5 | SCENE= }}
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'''Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2angstroms'''
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===Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2angstroms===
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==Overview==
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Bacteria synthesize fatty acids in a dissociated type pathway different from that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final step of fatty acid elongation, has been validated as a potential anti-microbial drug target. Triclosan is known to inhibit this enzyme effectively. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from five different species, one plant and four of microbial origin, have been examined in the available crystal structures. A comparison of these structures shows major structural differences at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated.
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The line below this paragraph, {{ABSTRACT_PUBMED_15381426}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15381426 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15381426}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for the variation in triclosan affinity to enoyl reductases., Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K, J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15381426 15381426]
Structural basis for the variation in triclosan affinity to enoyl reductases., Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K, J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15381426 15381426]
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Kinetic and structural analysis of the increased affinity of enoyl-ACP (acyl-carrier protein) reductase for triclosan in the presence of NAD+., Kapoor M, Mukhi PL, Surolia N, Suguna K, Surolia A, Biochem J. 2004 Aug 1;381(Pt 3):725-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15125687 15125687]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: P falciparum]]
[[Category: P falciparum]]
[[Category: Triclosan]]
[[Category: Triclosan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:13:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:48:19 2008''

Revision as of 19:48, 28 July 2008

Image:1uh5.png

Template:STRUCTURE 1uh5

Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2angstroms

Template:ABSTRACT PUBMED 15381426

About this Structure

1UH5 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.

Reference

Structural basis for the variation in triclosan affinity to enoyl reductases., Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K, J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:15381426

Kinetic and structural analysis of the increased affinity of enoyl-ACP (acyl-carrier protein) reductase for triclosan in the presence of NAD+., Kapoor M, Mukhi PL, Surolia N, Suguna K, Surolia A, Biochem J. 2004 Aug 1;381(Pt 3):725-33. PMID:15125687

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