1c14

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[[Image:1c14.gif|left|200px]]<br /><applet load="1c14" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1c14.gif|left|200px]]
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caption="1c14, resolution 2.0&Aring;" />
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'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX'''<br />
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{{Structure
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|PDB= 1c14 |SIZE=350|CAPTION= <scene name='initialview01'>1c14</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1C14 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=TCL:'>TCL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C14 OCA].
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1C14 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C14 OCA].
==Reference==
==Reference==
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Molecular basis for triclosan activity involves a flipping loop in the active site., Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS, Protein Sci. 1999 Nov;8(11):2529-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10595560 10595560]
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Molecular basis for triclosan activity involves a flipping loop in the active site., Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS, Protein Sci. 1999 Nov;8(11):2529-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10595560 10595560]
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: triclosan]]
[[Category: triclosan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:29 2008''

Revision as of 08:18, 20 March 2008

Image:1c14.gif


PDB ID 1c14

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: and
Activity: [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX


Overview

The crystal structure of the Escherichia coli enoyl reductase-NAD+-triclosan complex has been determined at 2.5 A resolution. The Ile192-Ser198 loop is either disordered or in an open conformation in the previously reported structures of the enzyme. This loop adopts a closed conformation in our structure, forming van der Waals interactions with the inhibitor and hydrogen bonds with the bound NAD+ cofactor. The opening and closing of this flipping loop is likely an important factor in substrate or ligand recognition. The closed conformation of the loop appears to be a critical feature for the enhanced binding potency of triclosan, and a key component in future structure-based inhibitor design.

About this Structure

1C14 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular basis for triclosan activity involves a flipping loop in the active site., Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS, Protein Sci. 1999 Nov;8(11):2529-32. PMID:10595560 [[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]

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