1muh
From Proteopedia
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|PDB= 1muh |SIZE=350|CAPTION= <scene name='initialview01'>1muh</scene>, resolution 2.30Å | |PDB= 1muh |SIZE=350|CAPTION= <scene name='initialview01'>1muh</scene>, resolution 2.30Å | ||
|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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1muh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1muh OCA], [http://www.ebi.ac.uk/pdbsum/1muh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1muh RCSB]</span> | ||
}} | }} | ||
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[[Category: Reznikoff, W S.]] | [[Category: Reznikoff, W S.]] | ||
[[Category: Thoden, J B.]] | [[Category: Thoden, J B.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: MN]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
[[Category: ribonuclease h-like motif]] | [[Category: ribonuclease h-like motif]] | ||
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[[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 22:21:15 2008'' |
Revision as of 19:21, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF TN5 TRANSPOSASE COMPLEXED WITH TRANSPOSON END DNA
Overview
Genomic evolution has been profoundly influenced by DNA transposition, a process whereby defined DNA segments move freely about the genome. Transposition is mediated by transposases, and similar events are catalyzed by retroviral integrases such as human immunodeficiency virus-1 (HIV-1) integrase. Understanding how these proteins interact with DNA is central to understanding the molecular basis of transposition. We report the three-dimensional structure of prokaryotic Tn5 transposase complexed with Tn5 transposon end DNA determined to 2.3 angstrom resolution. The molecular assembly is dimeric, where each double-stranded DNA molecule is bound by both protein subunits, orienting the transposon ends into the active sites. This structure provides a molecular framework for understanding many aspects of transposition, including the binding of transposon end DNA by one subunit and cleavage by a second, cleavage of two strands of DNA by a single active site via a hairpin intermediate, and strand transfer into target DNA.
About this Structure
1MUH is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1F3I. The following page contains interesting information on the relation of 1MUH with [Transposase]. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the Tn5 synaptic complex transposition intermediate., Davies DR, Goryshin IY, Reznikoff WS, Rayment I, Science. 2000 Jul 7;289(5476):77-85. PMID:10884228
Page seeded by OCA on Sun Mar 30 22:21:15 2008
