3m6z

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<StructureSection load='3m6z' size='340' side='right'caption='[[3m6z]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='3m6z' size='340' side='right'caption='[[3m6z]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3m6z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Metka Metka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M6Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3m6z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri_AV19 Methanopyrus kandleri AV19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M6Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m6k|3m6k]], [[3m7d|3m7d]], [[3m7g|3m7g]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MK1436, top5, Topoisomerase V ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190192 METKA])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6z OCA], [https://pdbe.org/3m6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m6z RCSB], [https://www.ebi.ac.uk/pdbsum/3m6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6z ProSAT]</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=3m6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6z OCA], [https://pdbe.org/3m6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m6z RCSB], [https://www.ebi.ac.uk/pdbsum/3m6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m6z ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q977W1_9EURY Q977W1_9EURY]
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Topoisomerase V is an archaeal type I topoisomerase that is unique among topoisomerases due to presence of both topoisomerase and DNA repair activities in the same protein. It is organized as an N-terminal topoisomerase domain followed by 24 tandem helix-hairpin-helix (HhH) motifs. Structural studies have shown that the active site is buried by the (HhH) motifs. Here we show that the N-terminal domain can relax DNA in the absence of any HhH motifs and that the HhH motifs are required for stable protein-DNA complex formation. Crystal structures of various topoisomerase V fragments show changes in the relative orientation of the domains mediated by a long bent linker helix, and these movements are essential for the DNA to enter the active site. Phosphate ions bound to the protein near the active site helped model DNA in the topoisomerase domain and show how topoisomerase V may interact with DNA.
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Structures of minimal catalytic fragments of topoisomerase v reveals conformational changes relevant for DNA binding.,Rajan R, Taneja B, Mondragon A Structure. 2010 Jul 14;18(7):829-38. PMID:20637419<ref>PMID:20637419</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3m6z" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Metka]]
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[[Category: Methanopyrus kandleri AV19]]
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[[Category: Mondragon, A]]
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[[Category: Mondragon A]]
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[[Category: Rajan, R]]
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[[Category: Rajan R]]
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[[Category: Taneja, B]]
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[[Category: Taneja B]]
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[[Category: Conformational changes in protein]]
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[[Category: Helix-hairpin-helix]]
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[[Category: Isomerase]]
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[[Category: Topoisomerase]]
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Revision as of 08:47, 7 February 2024

Crystal structure of an N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride

PDB ID 3m6z

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