Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions-Reference-Cited by-同舟云学术

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Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions

Published:2014-12-26 Issue:4 Volume:24 Page:495-507
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ebert Maximilian C. C. J. C.¹²³,Morley Krista L.²⁴,Volpato Jordan P.¹²,Schmitzer Andreea R.³⁴,Pelletier Joelle N.¹²³⁴

Affiliation:

1. Département de Biochimie; Université de Montréal; C.P. 6128, Succursale Centre-Ville Montréal Québec H3C 3J7 Canada

2. PROTEO, the Québec Network for Protein Function, Structure and Engineering; Québec Canada

3. CGCC, the Center for Green Chemistry and Catalysis; Montréal Canada

4. Département de Chimie; Université de Montréal; C.P. 6128, Succursale Centre-Ville Montréal Québec H3C 3J7 Canada

Funder

German Academic Exchange Service (DAAD); NSERC-Vanier Scholar; Natural Sciences and Engineering Research Council of Canada

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2602/fullpdf

Reference30 articles.

1. The emergence and spread of antibiotic resistance in food-borne bacteria;Threlfall;Int J Food Microbiol,2000

2. Crystal structure of a novel trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67;Matthews;Biochemistry,1986

3. Current status of the aadA and dfr gene cassette families;White;J Antimicrob Chemother,2001

4. Searching sequence space: two different approaches to dihydrofolate reductase catalysis;Howell;Chembiochem,2005

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2. A conserved SH3-like fold in diverse putative proteins tetramerizes into an oxidoreductase providing an antimicrobial resistance phenotype;Philosophical Transactions of the Royal Society B: Biological Sciences;2023-01-11

3. From a binding module to essential catalytic activity: how nature stumbled on a good thing;Chemical Communications;2023

4. The Bacterial Genomic Context of Highly Trimethoprim-Resistant DfrB Dihydrofolate Reductases Highlights an Emerging Threat to Public Health;Antibiotics;2021-04-13

5. Dual-Target Inhibitors of the Folate Pathway Inhibit Intrinsically Trimethoprim-Resistant DfrB Dihydrofolate Reductases;ACS Medicinal Chemistry Letters;2020-09-28

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