2bm6

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==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blanchard, J.S.]]
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[[Category: Blanchard, J S.]]
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[[Category: Hegde, S.S.]]
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[[Category: Hegde, S S.]]
[[Category: Maxwell, A.]]
[[Category: Maxwell, A.]]
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[[Category: Mitchenall, L.A.]]
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[[Category: Mitchenall, L A.]]
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[[Category: Roderick, S.L.]]
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[[Category: Roderick, S L.]]
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[[Category: Takiff, H.E.]]
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[[Category: Takiff, H E.]]
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[[Category: Vetting, M.W.]]
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[[Category: Vetting, M W.]]
[[Category: CS]]
[[Category: CS]]
[[Category: dna gyrase]]
[[Category: dna gyrase]]
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[[Category: right-handed quadrilateral beta-helix]]
[[Category: right-handed quadrilateral beta-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:25:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:16 2008''

Revision as of 14:39, 21 February 2008


2bm6, resolution 2.2Å

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

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 with as ligand. Known structural/functional Site: . 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

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