Biochemistry: A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA

Subray S. Hegde, Matthew W. Vetting, Steven L. Roderick, Lesley A. Mitchenall, Anthony Maxwell, Howard E. Takiff, John S. Blanchard

Research output: Contribution to journalArticle

191 Scopus citations

Abstract

Fluoroquinolones are gaining increasing importance in the treatment of tuberculosis. The expression of MfpA, a member of the pentapeptide repeat family of proteins from Mycobacterium tuberculosis, causes resistance to ciprofloxacin and sparfloxacin. This protein binds to DNA gyrase and inhibits its activity. Its three-dimensional structure reveals a fold, which we have named the right-handed quadrilateral β helix, that exhibits size, shape, and electrostatic similarity to B-form DNA. This represents a form of DNA mimicry and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo.

Original languageEnglish (US)
Pages (from-to)1480-1483
Number of pages4
JournalScience
Volume308
Issue number5727
DOIs
StatePublished - Jun 3 2005

ASJC Scopus subject areas

  • General

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