2VIC

CRYSTAL STRUCTURE OF THE ISHP608 TRANSPOSASE IN COMPLEX with Left end 26- mer DNA and manganese

Summary for 2VIC

• Entry DOI: 10.2210/pdb2vic/pdb
• Related: 2A6M 2A6O 2VHG 2VIH 2VJU 2VJV
• Descriptor: TRANSPOSASE ORFA, 5'-D(*AP*AP*AP*GP*CP*CP*CP*CP*TP*AP *GP*CP*TP*TP*TP*TP*AP*GP*CP*TP*AP*TP*GP*GP*GP*G)-3', MANGANESE (II) ION, ... (4 entities in total)
• Functional Keywords: dna-binding protein, protein-dna complex, huh motif, dna stem loop, transposition, dna binding protein
• Biological source: HELICOBACTER PYLORI; More
• Total number of polymer chains: 4
• Total formula weight: 52901.07

Authors

Barabas, O.,Ronning, D.R.,Guynet, C.,Hickman, A.B.,Ton-Hoang, B.,Chandler, M.,Dyda, F. (deposition date: 2007-11-29, release date: 2008-02-19, Last modification date: 2023-12-13)

Primary citation

Barabas, O.,Ronning, D.R.,Guynet, C.,Hickman, A.B.,Ton-Hoang, B.,Chandler, M.,Dyda, F.
Mechanism of is200/is605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection.
Cell(Cambridge,Mass.), 132:208-, 2008

PubMed Abstract: 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.

PubMed: 18243097
DOI: 10.1016/J.CELL.2007.12.029

Experimental method

X-RAY DIFFRACTION (2.35 Å)