2a6o: Difference between revisions

Revision as of 04:14, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a6o.png

Template:STRUCTURE 2a6o

Crystal Structure of the ISHp608 Transposase in Complex with Stem-loop DNACrystal Structure of the ISHp608 Transposase in Complex with Stem-loop DNA

Template:ABSTRACT PUBMED 16209952

About this StructureAbout this Structure

2A6O is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

Active site sharing and subterminal hairpin recognition in a new class of DNA transposases., Ronning DR, Guynet C, Ton-Hoang B, Perez ZN, Ghirlando R, Chandler M, Dyda F, Mol Cell. 2005 Oct 7;20(1):143-54. PMID:16209952

Page seeded by OCA on Tue Jul 29 04:14:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the ISHp608 Transposase in Complex with Stem-loop DNA'''
+===Crystal Structure of the ISHp608 Transposase in Complex with Stem-loop DNA===
-==Overview==
+<!--
-Many bacteria harbor simple transposable elements termed insertion sequences (IS). In Helicobacter pylori, the chimeric IS605 family elements are particularly interesting due to their proximity to genes encoding gastric epithelial invasion factors. Protein sequences of IS605 transposases do not bear the hallmarks of other well-characterized transposases. We have solved the crystal structure of full-length transposase (TnpA) of a representative member, ISHp608. Structurally, TnpA does not resemble any characterized transposase; rather, it is related to rolling circle replication (RCR) proteins. Consistent with RCR, Mg2+ and a conserved tyrosine, Tyr127, are essential for DNA nicking and the formation of a covalent intermediate between TnpA and DNA. TnpA is dimeric, contains two shared active sites, and binds two DNA stem loops representing the conserved inverted repeats near each end of ISHp608. The cocrystal structure with stem-loop DNA illustrates how this family of transposases specifically recognizes and pairs ends, necessary steps during transposition.
+The line below this paragraph, {{ABSTRACT_PUBMED_16209952}}, adds the Publication Abstract to the page
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 [[Category: Dna stem-loop]]
 [[Category: Rna recognition motif]]
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