2bm7: Difference between revisions

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-==THE STRUCTURE OF MFPA (RV3361C, P3221 CRYSTAL FORM). THE PENTAPEPTIDE REPEAT PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS FOLDS AS A RIGHT-HANDED QUADRILATERAL BETA-HELIX.==
-<StructureSection load='2bm7' size='340' side='right' caption='[[2bm7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+==The Structure of MfpA (Rv3361c, P3221 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.==
+<StructureSection load='2bm7' size='340' side='right'caption='[[2bm7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == 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 [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=2bm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm7 OCA], [https://pdbe.org/2bm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bm7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bm7 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O50390_MYCTO O50390_MYCTO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bm7_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bm7_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bm7 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== 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<ref>PMID:15933203</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium tuberculosis]]
+[[Category: Large Structures]]
-[[Category: Blanchard, J S]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Hegde, S S]]
+[[Category: Blanchard JS]]
-[[Category: Maxwell, A]]
+[[Category: Hegde SS]]
-[[Category: Mitchenall, L A]]
+[[Category: Maxwell A]]
-[[Category: Roderick, S L]]
+[[Category: Mitchenall LA]]
-[[Category: Takiff, H E]]
+[[Category: Roderick SL]]
-[[Category: Vetting, M W]]
+[[Category: Takiff HE]]
-[[Category: Dna gyrase]]
+[[Category: Vetting MW]]
-[[Category: Dna mimicry]]
-[[Category: Fluroquinolone resistance]]
-[[Category: Pentapeptide repeat protein]]
-[[Category: Right-handed quadrilateral beta-helix]]