2bm6

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[[Image:2bm6.gif|left|200px]]<br />
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[[Image:2bm6.gif|left|200px]]<br /><applet load="2bm6" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="2bm6" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2bm6, resolution 2.2&Aring;" />
caption="2bm6, resolution 2.2&Aring;" />
'''THE STRUCTURE OF MFPA (RV3361C, C2221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.'''<br />
'''THE STRUCTURE OF MFPA (RV3361C, C2221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.'''<br />
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==About this Structure==
==About this Structure==
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2BM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CS as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BM6 OCA].
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2BM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CS as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Cs Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BM6 OCA].
==Reference==
==Reference==
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[[Category: right-handed quadrilateral beta-helix]]
[[Category: right-handed quadrilateral beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:43:11 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:52:09 2007''

Revision as of 16:42, 18 December 2007


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 CS 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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