1mus
From Proteopedia
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- | [[Image:1mus.gif|left|200px]] | + | [[Image:1mus.gif|left|200px]] |
- | + | ||
- | '''crystal structure of Tn5 transposase complexed with resolved outside end DNA''' | + | {{Structure |
+ | |PDB= 1mus |SIZE=350|CAPTION= <scene name='initialview01'>1mus</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''crystal structure of Tn5 transposase complexed with resolved outside end DNA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1MUS is a [ | + | 1MUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1MUS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb84_1.html Transposase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUS OCA]. |
==Reference== | ==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:[http:// | + | Structure/function insights into Tn5 transposition., Steiniger-White M, Rayment I, Reznikoff WS, Curr Opin Struct Biol. 2004 Feb;14(1):50-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15102449 15102449] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transposase]] | [[Category: transposase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:25 2008'' |
Revision as of 10:48, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | , and | ||||||
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
Page seeded by OCA on Thu Mar 20 12:48:25 2008
Categories: Escherichia coli | Single protein | Transposase | Holden, H M. | Lovell, S. | Rayment, I. | Reznikoff, W S. | Steiniger-White, M. | Thoden, J B. | EDO | MG | MN | Dna binding | Hairpin