1c14: Difference between revisions
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[[Image:1c14.gif|left|200px]] | [[Image:1c14.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX''' | {{Structure | ||
|PDB= 1c14 |SIZE=350|CAPTION= <scene name='initialview01'>1c14</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene> | |||
|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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C14 is a [ | 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== | ||
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:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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| 1c14, resolution 2.0Å | |||||||||||||
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| Ligands: | NAD and TCL | ||||||||||||
| 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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