2bm7: Difference between revisions

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<StructureSection load='2bm7' size='340' side='right' caption='[[2bm7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2bm7' size='340' side='right' caption='[[2bm7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bm7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BM7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bm7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BM7 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bm4|2bm4]], [[2bm5|2bm5]], [[2bm6|2bm6]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bm4|2bm4]], [[2bm5|2bm5]], [[2bm6|2bm6]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bm7 RCSB], [http://www.ebi.ac.uk/pdbsum/2bm7 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm7 OCA], [http://pdbe.org/2bm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bm7 RCSB], [http://www.ebi.ac.uk/pdbsum/2bm7 PDBsum]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2bm7" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium tuberculosis]]
[[Category: Myctu]]
[[Category: Blanchard, J S]]
[[Category: Blanchard, J S]]
[[Category: Hegde, S S]]
[[Category: Hegde, S S]]

Revision as of 04:11, 12 September 2015

THE STRUCTURE OF MFPA (RV3361C, P3221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.THE STRUCTURE OF MFPA (RV3361C, P3221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.

Structural highlights

2bm7 is a 3 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Hegde SS, Vetting MW, Roderick SL, Mitchenall LA, Maxwell A, Takiff HE, Blanchard JS. A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA. Science. 2005 Jun 3;308(5727):1480-3. PMID:15933203 doi:308/5727/1480

2bm7, resolution 2.70Å

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OCA