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2BW3

Three-dimensional structure of the Hermes DNA transposase

Summary for 2BW3
Entry DOI10.2210/pdb2bw3/pdb
DescriptorTRANSPOSASE (3 entities in total)
Functional Keywordsdna recombination, transposition
Biological sourceMUSCA DOMESTICA (HOUSE FLY)
More
Total number of polymer chains2
Total formula weight71010.54
Authors
Hickman, A.B.,Perez, Z.N.,Zhou, L.,Musingarimi, P.,Ghirlando, R.,Hinshaw, J.E.,Craig, N.L.,Dyda, F. (deposition date: 2005-07-11, release date: 2005-07-28, Last modification date: 2024-11-13)
Primary citationHickman, A.B.,Perez, Z.N.,Zhou, L.,Musingarimi, P.,Ghirlando, R.,Hinshaw, J.E.,Craig, N.L.,Dyda, F.
Molecular Architecture of a Eukaryotic DNA Transposase
Nat.Struct.Mol.Biol., 12:715-, 2005
Cited by
PubMed Abstract: Mobile elements and their inactive remnants account for large proportions of most eukaryotic genomes, where they have had central roles in genome evolution. Over 50 years ago, McClintock reported a form of stress-induced genome instability in maize in which discrete DNA segments move between chromosomal locations. Our current mechanistic understanding of enzymes catalyzing transposition is largely limited to prokaryotic transposases. The Hermes transposon from the housefly is part of the eukaryotic hAT superfamily that includes hobo from Drosophila, McClintock's maize Activator and Tam3 from snapdragon. We report here the three-dimensional structure of a functionally active form of the transposase from Hermes at 2.1-A resolution. The Hermes protein has some structural features of prokaryotic transposases, including a domain with a retroviral integrase fold. However, this domain is disrupted by the insertion of an additional domain. Finally, transposition is observed only when Hermes assembles into a hexamer.
PubMed: 16041385
DOI: 10.1038/NSMB970
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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