2xma: Difference between revisions
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==DEINOCOCCUS RADIODURANS ISDRA2 TRANSPOSASE RIGHT END DNA COMPLEX== | ==DEINOCOCCUS RADIODURANS ISDRA2 TRANSPOSASE RIGHT END DNA COMPLEX== | ||
<StructureSection load='2xma' size='340' side='right' caption='[[2xma]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2xma' size='340' side='right'caption='[[2xma]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xma]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2xma]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XMA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xma OCA], [https://pdbe.org/2xma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xma RCSB], [https://www.ebi.ac.uk/pdbsum/2xma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xma ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DRA2A_DEIRA DRA2A_DEIRA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Transposase|Transposase]] | *[[Transposase 3D structures|Transposase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiodurans]] | ||
[[Category: Barabas | [[Category: Large Structures]] | ||
[[Category: Chandler | [[Category: Barabas O]] | ||
[[Category: Dyda | [[Category: Chandler M]] | ||
[[Category: Hickman | [[Category: Dyda F]] | ||
[[Category: James | [[Category: Hickman AB]] | ||
[[Category: Pasternak | [[Category: James JA]] | ||
[[Category: Sommer | [[Category: Pasternak C]] | ||
[[Category: Ton-Hoang | [[Category: Sommer S]] | ||
[[Category: Ton-Hoang B]] | |||
Latest revision as of 11:01, 23 August 2023
DEINOCOCCUS RADIODURANS ISDRA2 TRANSPOSASE RIGHT END DNA COMPLEXDEINOCOCCUS RADIODURANS ISDRA2 TRANSPOSASE RIGHT END DNA COMPLEX
Structural highlights
FunctionPublication Abstract from PubMedBacterial insertion sequences (ISs) from the IS200/IS605 family encode the smallest known DNA transposases and mobilize through single-stranded DNA transposition. Transposition by one particular family member, ISDra2 from Deinococcus radiodurans, is dramatically stimulated upon massive gamma irradiation. We have determined the crystal structures of four ISDra2 transposase/IS end complexes; combined with in vivo activity assays and fluorescence anisotropy binding measurements, these have revealed the molecular basis of strand discrimination and transposase action. The structures also show that previously established structural rules of target site recognition that allow different specific sequences to be targeted are only partially conserved among family members. Furthermore, we have captured a fully assembled active site including the scissile phosphate bound by a divalent metal ion cofactor (Cd(2+)) that supports DNA cleavage. Finally, the observed active site rearrangements when the transposase binds a metal ion in which it is inactive provide a clear rationale for metal ion specificity. DNA recognition and the precleavage state during single-stranded DNA transposition in D. radiodurans.,Hickman AB, James JA, Barabas O, Pasternak C, Ton-Hoang B, Chandler M, Sommer S, Dyda F EMBO J. 2010 Oct 1. PMID:20890269[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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