This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bm5
From Proteopedia
(New page: 200px<br /> <applet load="2bm5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bm5, resolution 2.0Å" /> '''THE STRUCTURE OF MFP...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BM5 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 SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BM5 OCA]]. | + | 2BM5 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 SO4 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=2BM5 OCA]]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 28: | ||
[[Category: right-handed quadrilateral beta-helix]] | [[Category: right-handed quadrilateral beta-helix]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:05:33 2007'' |
Revision as of 10:00, 30 October 2007
|
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] with SO4 as [ligand]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 12:05:33 2007
