2bm6: Difference between revisions

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[[Image:2bm6.gif|left|200px]]
{{Seed}}
[[Image:2bm6.png|left|200px]]


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{{STRUCTURE_2bm6|  PDB=2bm6  |  SCENE=  }}  
{{STRUCTURE_2bm6|  PDB=2bm6  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15933203}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15933203 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15933203}}


==About this Structure==
==About this Structure==
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[[Category: Pentapeptide repeat protein,fluroquinolone resistance]]
[[Category: Pentapeptide repeat protein,fluroquinolone resistance]]
[[Category: Right-handed quadrilateral beta-helix]]
[[Category: Right-handed quadrilateral beta-helix]]
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