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

Burk DL; Xiong B; Breitbach CBerghuis AM

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

机译：氨基糖苷类乙酰转移酶结构AAC(6’)——在一种新颖的水晶形式:结构性的和正常模式分析。

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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.

机译：aminoglycoside-modifying酶的氨基糖苷类6 -N-acetyltransferase Ii型(AAC(6)——]与代数余子式辅酶A的结晶空间群C222(1),一个晶胞参数= 71.5, b = 127.4, c = 76.9和1生理相关二聚体物种每不对称单元。观察了这个复杂的P2 (1) 2 (1) 2 (1)两个二聚体/不对称单位。六个可用的原体结构AAC (6) -Ii-CoA复杂,可能确定区域内的可塑性蛋白质。表明,这种可塑性不是一件人工制品crystal-packing部队,但该地区的显示的原体多种构象本质上是灵活的。的灵活性是相关合作酶的活动观察。

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《Acta crystallographica.Section D. Biological crystallography》 |2005年第9期|1273-1279|共7页
作者
Burk DL; Xiong B; Breitbach CBerghuis AM;
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作者单位

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

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正文语种英语
中图分类化学;
关键词
aminoglycoside acetyltransferase; Protomers; crystal outlinealginic acid;

机译：氨基糖苷类乙酰转移酶;原体晶体outlinealginic酸;

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

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