1suu: Difference between revisions

New page: left|200px<br /><applet load="1suu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1suu, resolution 1.75Å" /> '''Structure of DNA gyr...
 
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[[Image:1suu.gif|left|200px]]<br /><applet load="1suu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1suu, resolution 1.75&Aring;" />
'''Structure of DNA gyrase A C-terminal domain'''<br />


==Overview==
==Structure of DNA gyrase A C-terminal domain==
DNA gyrase is unique among enzymes for its ability to actively introduce, negative supercoils into DNA. This function is mediated in part by the, C-terminal domain of its A subunit (GyrA CTD). Here, we report the crystal, structure of this approximately 35-kDa domain determined to 1.75-A, resolution. The GyrA CTD unexpectedly adopts an unusual fold, which we, term a beta-pinwheel, that is globally reminiscent of a beta-propeller but, is built of blades with a previously unobserved topology. A large, conserved basic patch on the outer edge of this domain suggests a likely, site for binding and bending DNA; fluorescence resonance energy, transfer-based assays show that the GyrA CTD is capable of bending DNA by, &gt; or =180 degrees over a 40-bp region. Surprisingly, we find that the CTD, of the topoisomerase IV A subunit, which shares limited sequence homology, with the GyrA CTD, also bends DNA. Together, these data provide a physical, explanation for the ability of DNA gyrase to constrain a positive, superhelical DNA wrap, and also suggest that the particular substrate, preferences of topoisomerase IV might be dictated in part by the function, of this domain.
<StructureSection load='1suu' size='340' side='right'caption='[[1suu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1suu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=1suu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suu OCA], [https://pdbe.org/1suu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suu RCSB], [https://www.ebi.ac.uk/pdbsum/1suu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GYRA_BORBU GYRA_BORBU] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity).
== 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/su/1suu_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/main_output.php?pdb_ID=1suu ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SUU OCA].
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
 
__TOC__
==Reference==
</StructureSection>
The C-terminal domain of DNA gyrase A adopts a DNA-bending beta-pinwheel fold., Corbett KD, Shultzaberger RK, Berger JM, Proc Natl Acad Sci U S A. 2004 May 11;101(19):7293-8. Epub 2004 May 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15123801 15123801]
[[Category: Borreliella burgdorferi]]
[[Category: Borrelia burgdorferi]]
[[Category: Large Structures]]
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
[[Category: Berger JM]]
[[Category: Single protein]]
[[Category: Corbett KD]]
[[Category: Berger, J.M.]]
[[Category: Shultzaberger RK]]
[[Category: Corbett, K.D.]]
[[Category: Shultzaberger, R.K.]]
[[Category: beta-pinwheel]]
[[Category: beta-propeller]]
[[Category: dna gyrase]]
[[Category: topoisomerase]]
 
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