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==Mycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domain==
==Mycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domain==
<StructureSection load='3uc1' size='340' side='right' caption='[[3uc1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3uc1' size='340' side='right'caption='[[3uc1]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3uc1]] is a 1 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=3UC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UC1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3uc1]] is a 1 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=3UC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UC1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.65&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gyrA, MRA_0006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3uc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uc1 OCA], [https://pdbe.org/3uc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uc1 RCSB], [https://www.ebi.ac.uk/pdbsum/3uc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uc1 ProSAT]</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=3uc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uc1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uc1 RCSB], [http://www.ebi.ac.uk/pdbsum/3uc1 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A5TY74_MYCTA A5TY74_MYCTA]] 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.[HAMAP-Rule:MF_01897]
[https://www.uniprot.org/uniprot/GYRA_MYCTU GYRA_MYCTU] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA topoisomerases are essential enzymes that can overwind, underwind, and disentangle double-helical DNA segments to maintain the topological state of chromosomes. Nearly all bacteria utilize a unique type II topoisomerase, gyrase, which actively adds negative supercoils to chromosomes using an ATP-dependent DNA strand passage mechanism; however, the specific activities of these enzymes can vary markedly from species to species. E. coli gyrase is known to favor supercoiling over decatenation (1), whereas the opposite has been reported for Mycobacterium tuberculosis (Mtb) gyrase (2). Here, we set out to understand the molecular basis for these differences using structural and biochemical approaches. Contrary to expectations based on phylogenetic inferences (3), we find that the dedicated DNA wrapping domains (the CTDs) of both gyrases are highly similar, both architecturally and in their ability to introduce writhe into DNA. However, the Mtb enzyme lacks a C-terminal control element recently uncovered in E. coli gyrase (see accompanying paper), and turns over ATP at a much slower rate. Together, these findings demonstrate that CTD shape is not the sole regulatory determinant of gyrase activity, and instead indicate that an inability to tightly couple DNA wrapping to ATP turnover is why Mtb gyrase cannot supercoil DNA to the same extent as its gamma-proteobacterial counterpart. Our observations demonstrate that gyrase has been modified in multiple ways throughout evolution to fine-tune its specific catalytic properties.
 
Mechanisms For Defining Supercoiling Setpoint By DNA Gyrase Orthologs II. The shape of the GyrA CTD is not a sole determinant for controlling supercoiling efficiency.,Tretter EM, Berger JM J Biol Chem. 2012 Mar 28. PMID:22457352<ref>PMID:22457352</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Gyrase|Gyrase]]
*[[Gyrase 3D Structures|Gyrase 3D Structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium tuberculosis]]
[[Category: Large Structures]]
[[Category: Berger, J M]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Tretter, E M]]
[[Category: Berger JM]]
[[Category: Dna binding protein]]
[[Category: Tretter EM]]
[[Category: Gyrase]]
[[Category: Isomerase]]
[[Category: Topoisomerase]]

Latest revision as of 13:19, 1 March 2024

Mycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domainMycobacterium tuberculosis gyrase type IIA topoisomerase C-terminal domain

Structural highlights

3uc1 is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GYRA_MYCTU 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.

See Also

3uc1, resolution 1.65Å

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