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• W2002522402 abstract "IS200 transposases, present in many bacteria and Archaea, appear to be distinct from other groups of transposases. To provide a structural basis for understanding the action of IS200 transposases, we have determined the crystal structure of the SSO1474 protein from <i>Sulfolobus solfataricus</i>, a member of the IS200 family, in both Mn²⁺-bound and Mn²⁺-free forms. Its monomer fold is distinct from other classes of structurally characterized transposases. Two monomers form a tight dimer by exchanging the C-terminal α-helix and by merging the two central β-sheets into a large β-sheet. Glu⁵⁵, His⁶², and four water molecules provide the direct coordination sphere of the catalytically essential metal ion in the Mn²⁺-bound structure. His¹⁶, Asp⁵⁹, and His⁶⁰ also play important roles in maintaining the metal binding site. The catalytic site is formed at the interface between monomers. The candidate nucleophile in the transposition mechanism, strictly conserved Tyr¹²¹ coming from the other monomer, is turned away from the active site, suggesting that a conformational change is likely to occur during the catalytic cycle." @default.
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• W2002522402 date "2006-02-01" @default.
• W2002522402 modified "2023-10-18" @default.
• W2002522402 title "Crystal Structure of a Metal Ion-bound IS200 Transposase" @default.
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• W2002522402 doi "https://doi.org/10.1074/jbc.m511567200" @default.
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