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Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1273-9. Epub 2005 Aug 16.

Structures of aminoglycoside acetyltransferase AAC(6')-Ii in a novel crystal form: structural and normal-mode analyses.

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Department of Biochemistry, McGill University, 740 Dr Penfield Avenue, Montreal, QC, H3A 1A4, Canada.


The aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase type Ii [AAC(6')-Ii] has been crystallized with its cofactor coenzyme A in space group C222(1), with unit-cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit. The space group previously observed for this complex was P2(1)2(1)2(1), with two dimers per asymmetric unit. By comparing the six available protomer structures of the AAC(6')-Ii-CoA complex, it has been possible to identify regions of plasticity within the protein. Normal-mode analysis of this complex suggests that this plasticity is not an artefact of crystal-packing forces, but that the region of the protomer that displays multiple conformations is intrinsically flexible. It is conjectured that the flexibility is relevant for the cooperative activity observed for the enzyme.

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