2bm5
From Proteopedia
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|PDB= 2bm5 |SIZE=350|CAPTION= <scene name='initialview01'>2bm5</scene>, resolution 2.0Å | |PDB= 2bm5 |SIZE=350|CAPTION= <scene name='initialview01'>2bm5</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm5 OCA], [http://www.ebi.ac.uk/pdbsum/2bm5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bm5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Takiff, H E.]] | [[Category: Takiff, H E.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
| - | [[Category: SO4]] | ||
[[Category: dna gyrase]] | [[Category: dna gyrase]] | ||
[[Category: dna mimicry]] | [[Category: dna mimicry]] | ||
| - | + | [[Category: pentapeptide repeat protein,fluroquinolone resistance]] | |
| - | [[Category: pentapeptide repeat protein]] | + | |
[[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 Mon Mar 31 02:08:26 2008'' |
Revision as of 23:08, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF MFPA (RV3361C, P21 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
2BM5 is a Single protein structure of sequence from Mycobacterium tuberculosis. 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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