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2vih

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Revision as of 11:38, 30 March 2022

CRYSTAL STRUCTURE OF THE IS608 TRANSPOSASE IN COMPLEX WITH Left END 26-MER DNA

Structural highlights

2vih is a 4 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2vhg, 2a6m, 2a6o
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The smallest known DNA transposases are those from the IS200/IS605 family. Here we show how the interplay of protein and DNA activates TnpA, the Helicobacter pylori IS608 transposase, for catalysis. First, transposon end binding causes a conformational change that aligns catalytically important protein residues within the active site. Subsequent precise cleavage at the left and right ends, the steps that liberate the transposon from its donor site, does not involve a site-specific DNA-binding domain. Rather, cleavage site recognition occurs by complementary base pairing with a TnpA-bound subterminal transposon DNA segment. Thus, the enzyme active site is constructed from elements of both protein and DNA, reminiscent of the interdependence of protein and RNA in the ribosome. Our structural results explain why the transposon ends are asymmetric and how the transposon selects a target site for integration, and they allow us to propose a molecular model for the entire transposition reaction.

Mechanism of IS200/IS605 family DNA transposases: activation and transposon-directed target site selection.,Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F Cell. 2008 Jan 25;132(2):208-20. PMID:18243097^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F. Mechanism of IS200/IS605 family DNA transposases: activation and transposon-directed target site selection. Cell. 2008 Jan 25;132(2):208-20. PMID:18243097 doi:http://dx.doi.org/10.1016/j.cell.2007.12.029

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vih"

@@ Line 3: / Line 3: @@
 <StructureSection load='2vih' size='340' side='right'caption='[[2vih]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vih]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VIH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vih]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIH FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vhg|2vhg]], [[2a6m|2a6m]], [[2a6o|2a6o]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vhg|2vhg]], [[2a6m|2a6m]], [[2a6o|2a6o]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vih OCA], [http://pdbe.org/2vih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vih RCSB], [http://www.ebi.ac.uk/pdbsum/2vih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vih 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=2vih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vih OCA], [https://pdbe.org/2vih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vih RCSB], [https://www.ebi.ac.uk/pdbsum/2vih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vih ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2vih

From Proteopedia

Revision as of 11:38, 30 March 2022

CRYSTAL STRUCTURE OF THE IS608 TRANSPOSASE IN COMPLEX WITH Left END 26-MER DNA

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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