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Published online before print April 9, 2004, 10.1110/ps.03585004
Protein Science (2004), 13:1260-1265. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Structure of fosfomycin resistance protein FosA from transposon Tn2921

Svetlana Pakhomova1, Chris L. Rife2, Richard N. Armstrong2 and Marcia E. Newcomer1

1 Departments of Biological Sciences and Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803, USA
2 Departments of Biochemistry and Chemistry, Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA

(RECEIVED December 23, 2003; FINAL REVISION February 4, 2004; ACCEPTED February 4, 2004)



Abstract

The crystal structure of fosfomycin resistance protein FosA from transposon Tn2921 has been established at a resolution of 2.5 Å. The protein crystallized without bound Mn(II) and K+, ions crucial for efficient catalysis, providing a structure of the apo enzyme. The protein maintains the three-dimensional domain-swapped arrangement of the paired {beta}{alpha}{beta}{beta}{beta}-motifs observed in the genomically encoded homologous enzyme from Pseudomonas aeruginosa (PA1129). The basic architecture of the active site is also maintained, despite the absence of the catalytically essential Mn(II). However, the absence of K+, which has been shown to enhance enzymatic activity, appears to contribute to conformational heterogeneity in the K+-binding loops.

Keywords: fosfomycin; fosfomycin resistance protein FosA; antibiotic resistance; X-ray crystallography

Abbreviations: FosA, fosfomycin resistance protein from transposon Tn2921 • PA1129, fosfomycin resistance protein from PA1129 gene from P. aeruginosa • GSH, glutathioneK+ loop, potassium binding loop • RMSD, root-mean-square deviation • NCS, noncrystallographic symmetry • VOC, vicinal chelate superfamily of enzymes

Reprints requests to: Svetlana Pakhomova, Department of Biological Sciences, Life Sciences Building, Room 202, Louisiana State University, Baton Rouge, LA 70803, USA; e-mail:e-mail:sveta{at}lsu.edu; fax: (225) 578-7258.

Article published ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03585004.


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