1suu

<StructureSection load='1suu' size='340' side='right' caption='[[1suu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1suu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SUU FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYRA, BB0435 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 ATCC 35210])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=1suu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suu OCA], [http://pdbe.org/1suu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1suu RCSB], [http://www.ebi.ac.uk/pdbsum/1suu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1suu ProSAT]</span></td></tr>

[[http://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).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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:15123801<ref>PMID:15123801</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1suu" style="background-color:#fffaf0;"></div>

*[[Gyrase|Gyrase]]

[[Category: Atcc 35210]]

[[Category: Berger, J M]]

[[Category: Corbett, K D]]

[[Category: Shultzaberger, R K]]

[[Category: Beta-pinwheel]]

[[Category: Topoisomerase]]