2BM5

The Structure of MfpA (Rv3361c, P21 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.

Summary for 2BM5

• Entry DOI: 10.2210/pdb2bm5/pdb
• Related: 2BM4 2BM6 2BM7
• Descriptor: PENTAPEPTIDE REPEAT FAMILY PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: pentapeptide repeat protein, fluroquinolone resistance, dna gyrase, dna mimicry, right-handed quadrilateral beta-helix
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 2
• Total formula weight: 40747.78

Authors

Hegde, S.S.,Vetting, M.W.,Roderick, S.L.,Mitchenall, L.A.,Maxwell, A.,Takiff, H.E.,Blanchard, J.S. (deposition date: 2005-03-09, release date: 2005-06-07, Last modification date: 2024-05-01)

Primary citation

Hegde, S.S.,Vetting, M.W.,Roderick, S.L.,Mitchenall, L.A.,Maxwell, A.,Takiff, H.E.,Blanchard, J.S.
A Fluroquinolone Resistance Protein from Mycobacterium Tuberculosis that Mimics DNA
Science, 308:1480-, 2005

PubMed 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 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.

PubMed: 15933203
DOI: 10.1126/SCIENCE.1110699

Experimental method

X-RAY DIFFRACTION (2 Å)