2bm6 | pdb_00002bm6
THE STRUCTURE OF MFPA (RV3361C, C2221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.
| |||||||||||||
| 2bm6, resolution 2.2Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | CS | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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 Structure
2BM6 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:03:44 2008
