1mus
From Proteopedia
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|PDB= 1mus |SIZE=350|CAPTION= <scene name='initialview01'>1mus</scene>, resolution 1.90Å | |PDB= 1mus |SIZE=350|CAPTION= <scene name='initialview01'>1mus</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mur|1MUR]] | ||
| + | |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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[[Category: Steiniger-White, M.]] | [[Category: Steiniger-White, M.]] | ||
[[Category: Thoden, J B.]] | [[Category: Thoden, J B.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: MN]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: hairpin]] | [[Category: hairpin]] | ||
[[Category: transposase]] | [[Category: transposase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:26 2008'' |
Revision as of 19:21, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Related: | 1MUR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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