1mus

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[[Image:1mus.gif|left|200px]]
[[Image:1mus.gif|left|200px]]
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{{Structure
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|PDB= 1mus |SIZE=350|CAPTION= <scene name='initialview01'>1mus</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1mus", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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{{STRUCTURE_1mus| PDB=1mus | SCENE= }}
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|RELATEDENTRY=[[1mur|1MUR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mus OCA], [http://www.ebi.ac.uk/pdbsum/1mus PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mus RCSB]</span>
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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: dna binding]]
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[[Category: Dna binding]]
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[[Category: hairpin]]
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[[Category: Hairpin]]
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[[Category: transposase]]
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[[Category: Transposase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:44:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:26 2008''
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Revision as of 22:44, 2 May 2008

Image:1mus.gif

Template:STRUCTURE 1mus

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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