2bm7: Difference between revisions
New page: left|200px<br /><applet load="2bm7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bm7, resolution 2.7Å" /> '''THE STRUCTURE OF MFPA... |
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==Overview== | ==Overview== | ||
Fluoroquinolones are gaining increasing importance in the treatment of | 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== | ==About this Structure== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blanchard, J | [[Category: Blanchard, J S.]] | ||
[[Category: Hegde, S | [[Category: Hegde, S S.]] | ||
[[Category: Maxwell, A.]] | [[Category: Maxwell, A.]] | ||
[[Category: Mitchenall, L | [[Category: Mitchenall, L A.]] | ||
[[Category: Roderick, S | [[Category: Roderick, S L.]] | ||
[[Category: Takiff, H | [[Category: Takiff, H E.]] | ||
[[Category: Vetting, M | [[Category: Vetting, M W.]] | ||
[[Category: dna gyrase]] | [[Category: dna gyrase]] | ||
[[Category: dna mimicry]] | [[Category: dna mimicry]] | ||
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[[Category: right-handed quadrilateral beta-helix]] | [[Category: right-handed quadrilateral beta-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:20 2008'' | ||
Revision as of 17:39, 21 February 2008
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THE STRUCTURE OF MFPA (RV3361C, P3221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.
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
2BM7 is a Single protein structure of sequence from Mycobacterium tuberculosis. 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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