Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Published online before print April 9, 2004
Protein Science, DOI: 10.1110/ps.03585004
 Copyright © 2004 The Protein Society
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.03585004v1
13/5/1260    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pakhomova, S.
Right arrow Articles by Newcomer, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pakhomova, S.
Right arrow Articles by Newcomer, M. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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, glutathione • K+ 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:sveta{at}lsu.edu; fax: (225) 578-7258.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03585004.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2004 by The Protein Society.