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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase.
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Introduction of a leucine half-zipper engenders multiple high-quality crystals of a recalcitrant tRNA synthetase.

机译：引入亮氨酸half-zipper产生多个高质量晶体的顽固的tRNA合成酶。

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摘要

Although Escherichia coli alanyl-tRNA synthetase was among the first tRNA synthetases to be sequenced and extensively studied by functional analysis, it has proved to be recalcitrant to crystallization. This challenge remained even for crystallization of the catalytic fragment. By mutationally introducing three stacked leucines onto the solvent-exposed side of an alpha-helix, an engineered catalytic fragment of the synthetase was obtained that yielded multiple high-quality crystals and cocrystals with different ligands. The engineered alpha-helix did not form a leucine zipper that interlocked with the same alpha-helix from another molecule. Instead, using the created hydrophobic spine, it interacted with other surfaces of the protein as a leucine half-zipper (LHZ) to enhance the crystal lattice interactions. The LHZ made crystal lattice contacts in all crystals of different space groups. These results illustrate the power of introducing an LHZ into helices to facilitate crystallization. The authors propose that the method can be unified with surface-entropy reduction and can be broadly used for protein-surface optimization in crystallization.
机译：尽管大肠杆菌alanyl-tRNA合成酶是最早tRNA合成酶是什么测序和广泛研究的功能分析,它已被证明是顽固的结晶。结晶的催化片段。突变引入三叠亮氨酸到solvent-exposed a螺旋,一个工程催化的片段获得了多个合成酶高质量的晶体和cocrystals不同的配体。没有形成一个连锁的亮氨酸拉链从另一个分子相同的阿尔法螺旋。相反,使用创建的疏水性的脊柱,它与其他表面蛋白质的相互作用一个亮氨酸half-zipper (LHZ)提高晶格相互作用。在所有晶体的晶格联系人不同的空间组织。将一个LHZ引入螺旋的力量促进结晶。该方法是可以统一起来的surface-entropy减少,可以广泛应用protein-surface优化的结晶。

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