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1mus
From Proteopedia
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[[Image:1mus.gif|left|200px]] | [[Image:1mus.gif|left|200px]] | ||
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'''crystal structure of Tn5 transposase complexed with resolved outside end DNA''' | '''crystal structure of Tn5 transposase complexed with resolved outside end DNA''' | ||
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[[Category: Steiniger-White, M.]] | [[Category: Steiniger-White, M.]] | ||
[[Category: Thoden, J B.]] | [[Category: Thoden, J B.]] | ||
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| - | [[Category: | + | [[Category: Hairpin]] |
| - | [[Category: | + | [[Category: Transposase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:44:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:44, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 01:44:45 2008
