3m6k
From Proteopedia
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| - | [[ | + | ==Crystal Structure of N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride== |
| + | <StructureSection load='3m6k' size='340' side='right' caption='[[3m6k]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3m6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M6K FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MK1436, top5, Topoisomerase V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2320 Methanopyrus kandleri])</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=3m6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m6k RCSB], [http://www.ebi.ac.uk/pdbsum/3m6k PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Topoisomerase|Topoisomerase]] | *[[Topoisomerase|Topoisomerase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Methanopyrus kandleri]] | [[Category: Methanopyrus kandleri]] | ||
| - | [[Category: Mondragon, A | + | [[Category: Mondragon, A]] |
| - | [[Category: Rajan, R | + | [[Category: Rajan, R]] |
| - | [[Category: Taneja, B | + | [[Category: Taneja, B]] |
[[Category: Conformational change in protein]] | [[Category: Conformational change in protein]] | ||
[[Category: Guanidium hydrochloride]] | [[Category: Guanidium hydrochloride]] | ||
Revision as of 09:53, 9 December 2014
Crystal Structure of N-terminal 44 kDa fragment of topoisomerase V in the presence of guanidium hydrochloride
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