1MUS

crystal structure of Tn5 transposase complexed with resolved outside end DNA

Summary for 1MUS

• Entry DOI: 10.2210/pdb1mus/pdb
• Related: 1MUR
• Descriptor: DNA transferred strand, DNA non-transferred strand, Tn5 transposase, ... (7 entities in total)
• Functional Keywords: transposase, hairpin, dna binding, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 65933.77

Authors

Holden, H.M.,Thoden, J.B.,Steiniger-White, M.,Reznikoff, W.S.,Lovell, S.,Rayment, I. (deposition date: 2002-09-24, release date: 2002-09-27, Last modification date: 2024-02-14)

Primary citation

Steiniger-White, M.,Rayment, I.,Reznikoff, W.S.
Structure/function insights into Tn5 transposition.
Curr.Opin.Struct.Biol., 14:50-57, 2004

PubMed Abstract: Prokaryotic transposon 5 (Tn5) serves as a model system for studying the molecular mechanism of DNA transposition. Elucidation of the X-ray co-crystal structure of Tn5 transposase complexed with a DNA recognition end sequence provided the first three-dimensional picture of an intermediate in a transposition/retroviral integration pathway. The many Tn5 transposase-DNA co-crystal structures now available complement biochemical and genetic studies, allowing a comprehensive and detailed understanding of transposition mechanisms. Specifically, the structures reveal two different types of protein-DNA contacts: cis contacts, required for initial DNA recognition, and trans contacts, required for catalysis. Protein-protein contacts required for synapsis are also seen. Finally, the two divalent metals in the active site of the transposase support a 'two-metal-ion' mechanism for Tn5 transposition.

PubMed: 15102449
DOI: 10.1016/j.sbi.2004.01.008

Experimental method

X-RAY DIFFRACTION (1.9 Å)