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The tip region of the MacA alpha-hairpin is important for the binding to TolC to the Escherichia coli MacAB-TolC pump
- Authors
- Xu, Yongbin; Sim, Se-Hoon; Song, Saemee; Piao, Shunfu; Kim, Hong-Man; Jin, Xiao Ling; Lee, Kangseok; Ha, Nam-Chul
- Issue Date
- Apr-2010
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Multidrug resistance; MacA; TolC; Assembly model
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.394, no.4, pp 962 - 965
- Pages
- 4
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 394
- Number
- 4
- Start Page
- 962
- End Page
- 965
- ISSN
- 0006-291X
1090-2104
- Abstract
- The tripartite efflux pump MacAB-TolC found in Gram-negative bacteria is involved in resistance to antibiotics. We previously reported the funnel-like hexameric structure of the adaptor protein MacA to be physiologically relevant. In this study, we investigated the role of the tip region of its alpha-hairpin, which forms a cogwheel structure in the funnel-like shape of the MacA hexamer. Mutational and biochemical analyses revealed that the conserved residues located at the tip region of the alpha-hairpin of MacA play an essential role in the binding of TolC. Our findings offer a molecular basis for understanding the drug resistance of pathogenic bacteria. (C) 2010 Elsevier Inc. All rights reserved.
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Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
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