1mus

From Proteopedia

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Revision as of 06:56, 18 November 2007

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spinqualitylabelsall models 1mus, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

crystal structure of Tn5 transposase complexed with resolved outside end DNA

Overview

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.

About this Structure

1MUS is a Single protein structure of sequence from Escherichia coli with MN, MG and EDO as ligands. The following page contains interesting information on the relation of 1MUS with [Transposase]. Full crystallographic information is available from OCA.

Reference

Structure/function insights into Tn5 transposition., Steiniger-White M, Rayment I, Reznikoff WS, Curr Opin Struct Biol. 2004 Feb;14(1):50-7. PMID:15102449

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