DOI: 10.1110/ps.8.11.2529. Molecular basis for triclosan activity involves a flipping loop in the active site

Molecular basis for triclosan activity involves a flipping loop in the active site

10.1110/ps.8.11.2529

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractThe crystal structure of the Escherichia coli enoyl reductase‐NAD +‐triclosan complex has been determined at 2.5 Å 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.

Bibliography

Qiu, X., AbdelâMeguid, S. S., Janson, C. A., Court, R. I., Smyth, M. G., & Payne, D. J. (1999). Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Science, 8(11), 2529â2532. Portico.

Authors 6

Xiayang Qiu (first)
Sherin S. Abdel‐Meguid (additional)
Cheryl A. Janson (additional)
Robert I. Court (additional)
Martin G. Smyth (additional)
David J. Payne (additional)

References 16 Referenced 98

10.1126/science.274.5295.2107
10.1006/jmbi.1998.2271
10.1016/S0196-6553(96)90017-6
{'key': 'e_1_2_1_5_1', 'volume-title': 'X‐PLOR version. 3.1, A system for X‐ray crystallography and NMR', 'author': 'Brünger AT', 'year': '1987'} / X‐PLOR version. 3.1, A system for X‐ray crystallography and NMR by Brünger AT (1987)
10.1111/j.1574-6968.2006.00441.x
10.1021/jm00374a003
10.1074/jbc.270.44.26538
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10.1038/273443a0
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10.1038/28970
10.1126/science.280.5369.1607
{'key': 'e_1_2_1_15_1', 'first-page': '427', 'article-title': 'Crystallization of the NADP‐dependent beta‐keto acyl carrier protein reductase from Escherichia coli', 'volume': '54', 'author': 'Rafferty JB', 'year': '1998', 'journal-title': 'Acta Crystallogr'} / Acta Crystallogr / Crystallization of the NADP‐dependent beta‐keto acyl carrier protein reductase from Escherichia coli by Rafferty JB (1998)
10.1016/S0969-2126(01)00227-1
10.1126/science.279.5347.98

Dates

Type	When
Created	16 years, 6 months ago (Feb. 17, 2009, 4:36 p.m.)
Deposited	1 year, 10 months ago (Oct. 28, 2023, 5:46 p.m.)
Indexed	1 month, 1 week ago (July 22, 2025, 6:54 a.m.)
Issued	26 years, 8 months ago (Jan. 1, 1999)
Published	26 years, 8 months ago (Jan. 1, 1999)
Published Online	16 years, 8 months ago (Dec. 31, 2008)
Published Print	26 years, 8 months ago (Jan. 1, 1999)

Funders 0

None

BibTeX

@article{Qiu_1999, title={Molecular basis for triclosan activity involves a flipping loop in the active site}, volume={8}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.8.11.2529}, DOI={10.1110/ps.8.11.2529}, number={11}, journal={Protein Science}, publisher={Wiley}, author={Qiu, Xiayang and Abdel‐Meguid, Sherin S. and Janson, Cheryl A. and Court, Robert I. and Smyth, Martin G. and Payne, David J.}, year={1999}, month=jan, pages={2529–2532} }

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