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1c14
From Proteopedia
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[[Image:1c14.gif|left|200px]] | [[Image:1c14.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1c14| PDB=1c14 | SCENE= }} |
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'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX''' | '''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX''' | ||
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==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://www.ncbi.nlm.nih.gov/pubmed/10595560 10595560] | 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: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Qiu, X.]] | [[Category: Qiu, X.]] | ||
[[Category: Smyth, M.]] | [[Category: Smyth, M.]] | ||
| - | [[Category: | + | [[Category: Enoyl reductase]] |
| - | [[Category: | + | [[Category: Fabi]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Triclosan]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:12:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:12, 2 May 2008
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 Page seeded by OCA on Fri May 2 12:12:17 2008
