2bm6

THE STRUCTURE OF MFPA (RV3361C, C2221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.

File:2bm6.gif

OverviewOverview

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 beta 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.

About this StructureAbout this Structure

2BM6 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with CS as [ligand]. Full crystallographic information is available from [OCA].

ReferenceReference

A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA., Hegde SS, Vetting MW, Roderick SL, Mitchenall LA, Maxwell A, Takiff HE, Blanchard JS, Science. 2005 Jun 3;308(5727):1480-3. PMID:15933203

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