1suu: Difference between revisions

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<StructureSection load='1suu' size='340' side='right'caption='[[1suu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1suu' size='340' side='right'caption='[[1suu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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://proteopedia.org/fgij/fg.htm?mol=1SUU FirstGlance]. <br>
<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='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>
</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='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'>[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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<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>


==See Also==
==See Also==
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35210]]
[[Category: Borreliella burgdorferi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berger, J M]]
[[Category: Berger JM]]
[[Category: Corbett, K D]]
[[Category: Corbett KD]]
[[Category: Shultzaberger, R K]]
[[Category: Shultzaberger RK]]
[[Category: Beta-pinwheel]]
[[Category: Beta-propeller]]
[[Category: Dna gyrase]]
[[Category: Isomerase]]
[[Category: Topoisomerase]]

Latest revision as of 11:34, 14 February 2024

Structure of DNA gyrase A C-terminal domainStructure of DNA gyrase A C-terminal domain

Structural highlights

1suu is a 1 chain structure with sequence from Borreliella burgdorferi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

See Also

1suu, resolution 1.75Å

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