Crystal Structure of a Genomically Encoded Fosfomycin Resistance Protein (FosA) at 1.19 Å Resolution by MAD Phasing Off the L-III Edge of Tl+-Reference-Cited by-同舟云学术

Crystal Structure of a Genomically Encoded Fosfomycin Resistance Protein (FosA) at 1.19 Å Resolution by MAD Phasing Off the L-III Edge of Tl+

Published:2002-08-20 Issue:37 Volume:124 Page:11001-11003
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Rife Chris L.¹,Pharris Rachel E.¹,Newcomer Marcia E.¹,Armstrong Richard N.¹

Affiliation:

1. Departments of Biochemistry and Chemistry, Vanderbilt University, Nashville, Tennessee 37232-0146, and Departments of Biological Sciences and Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja026879v

Reference22 articles.

1. Formation of an adduct between fosfomycin and glutathione: a new mechanism of antibiotic resistance in bacteria

2. Fosfomycin Resistance Protein (FosA) Is a Manganese Metalloglutathione Transferase Related to Glyoxalase I and the Extradiol Dioxygenases

3. Elucidation of a Monovalent Cation Dependence and Characterization of the Divalent Cation Binding Site of the Fosfomycin Resistance Protein (FosA)

4. Elementary Steps in the Acquisition of Mn2+ by the Fosfomycin Resistance Protein (FosA)

5. EPR Study of Substrate Binding to the Mn(II) Active Site of the Bacterial Antibiotic Resistance Enzyme FosA: A Better Way To Examine Mn(II)

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