2bm4 | pdb_00002bm4

THE STRUCTURE OF MFPA (RV3361C, C2 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.

spinqualitylabelsall models 2bm4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bm4 is a 2 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2bm5, 2bm6, 2bm7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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