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==Thermotoga maritima reverse gyrase, triclinic form==
==Thermotoga maritima reverse gyrase, triclinic form==
<StructureSection load='4ddv' size='340' side='right' caption='[[4ddv]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
<StructureSection load='4ddv' size='340' side='right'caption='[[4ddv]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ddv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DDV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DDV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ddv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DDV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.46&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ddt|4ddt]], [[4ddu|4ddu]], [[4ddw|4ddw]], [[4ddx|4ddx]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rgy, topR, TM_0173 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=4ddv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ddv OCA], [https://pdbe.org/4ddv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ddv RCSB], [https://www.ebi.ac.uk/pdbsum/4ddv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ddv 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=4ddv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ddv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ddv RCSB], [http://www.ebi.ac.uk/pdbsum/4ddv PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RGYR_THEMA RGYR_THEMA]] Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.  
[https://www.uniprot.org/uniprot/RGYR_THEMA RGYR_THEMA] Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Reverse gyrase is an ATP-dependent topoisomerase that is unique to hyperthermophilic archaea and eubacteria. The only reverse gyrase structure determined to date has revealed the arrangement of the N-terminal helicase domain and the C-terminal topoisomerase domain that intimately cooperate to generate the unique function of positive DNA supercoiling. Although the structure has elicited hypotheses as to how supercoiling may be achieved, it lacks structural elements important for supercoiling and the molecular mechanism of positive supercoiling is still not clear. We present five structures of authentic Thermotoga maritima reverse gyrase that reveal a first view of two interacting zinc fingers that are crucial for positive DNA supercoiling. The so-called latch domain, which connects the helicase and the topoisomerase domains is required for their functional cooperation and presents a novel fold. Structural comparison defines mobile regions in parts of the helicase domain, including a helical insert and the latch that are likely important for DNA binding during catalysis. We show that the latch, the helical insert and the zinc fingers contribute to the binding of DNA to reverse gyrase and are uniquely placed within the reverse gyrase structure to bind and guide DNA during strand passage. A possible mechanism for positive supercoiling by reverse gyrases is presented.
 
Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling.,Rudolph MG, Del Toro Duany Y, Jungblut SP, Ganguly A, Klostermeier D Nucleic Acids Res. 2012 Dec 2. PMID:23209025<ref>PMID:23209025</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]]
*[[Topoisomerase|Topoisomerase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Klostermeier, D]]
[[Category: Klostermeier D]]
[[Category: Rudolph, M G]]
[[Category: Rudolph MG]]
[[Category: Archaea]]
[[Category: Dna supercoiling]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Topoisomerase]]

Latest revision as of 17:32, 14 March 2024

Thermotoga maritima reverse gyrase, triclinic formThermotoga maritima reverse gyrase, triclinic form

Structural highlights

4ddv is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.46Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RGYR_THEMA Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.

See Also

4ddv, resolution 3.46Å

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