Literature summary for 2.7.7.B22 extracted from

Hickman, A.B.; Voth, A.R.; Ewis, H.; Li, X.; Craig, N.L.; Dyda, F.
Structural insights into the mechanism of double strand break formation by Hermes, a hAT family eukaryotic DNA transposase (2018), Nucleic Acids Res., 46, 10286-10301 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
cocrystal structures of the Hermes transposase bound to DNA that mimics the reaction step immediately prior to hairpin formation. A large DNA conformational change occurs between the initial cleavage step and subsequent hairpin formation that changes which strand is acted upon by a single active site. The complement of divalent metal ions bound by the catalytically essential DDE residues, and the identity of the -2 flanking base pair affect the conformationbal change. For efficient hairpin formation an A:T basepair is favored at the -2 position. The histidine residue within a conserved C/DxxH motif interacts directly with the scissile phosphate	Musca domestica

Crystallization (Comment)

Organism

cocrystal structures of the Hermes transposase bound to DNA that mimics the reaction step immediately prior to hairpin formation. A large DNA conformational change occurs between the initial cleavage step and subsequent hairpin formation that changes which strand is acted upon by a single active site. The complement of divalent metal ions bound by the catalytically essential DDE residues, and the identity of the -2 flanking base pair affect the conformationbal change. For efficient hairpin formation an A:T basepair is favored at the -2 position. The histidine residue within a conserved C/DxxH motif interacts directly with the scissile phosphate

Musca domestica

Organism

Organism	UniProt	Comment	Textmining
Musca domestica	Q25438	-	-

Synonyms

Synonyms	Comment	Organism
Hermes transposase	-	Musca domestica

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Release 2023.1 (January 2023)