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首页> 外文期刊>Journal of Biochemistry >Two Crystal Structures of Lysyl-tRNA Synthetase from Bacillus stearothermophilus in Complex with Lysyladenylate-Like Compounds: Insights into the Irreversible Formation of the Enzyme-Bound Adenylate of l-Lysine Hydroxamate
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Two Crystal Structures of Lysyl-tRNA Synthetase from Bacillus stearothermophilus in Complex with Lysyladenylate-Like Compounds: Insights into the Irreversible Formation of the Enzyme-Bound Adenylate of l-Lysine Hydroxamate

机译：嗜热脂肪芽孢杆菌的赖氨酰-tRNA合成酶的两个晶体结构与类似赖氨酰腺苷的化合物复合：对赖氨酸异羟肟酸酯酶结合的腺苷酸不可逆形成的见解。

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Aminoacyl-tRNA synthetase forms an enzyme-bound intermediate, aminoacyladenylate in the amino-acid activation reaction. This reaction is monitored by measuring the ATP-PPi exchange reason in which [32P]PPi is incorporated into ATP. We previously reported that l-lysine hydroxamate completely inhibited the l-lysine-dependent ATP-PPi exchange reaction catalysed by lysyl-tRNA synthetase from Bacillus stearothermophilus (BsLysRS). Several experiments suggested that BsLysRS can adenylate l-lysine hydroxamate, but the enzyme-bound lysyladenylate-like compound does not undergo the nucleophilic attack of PPi. This contrasts with the two reports for seryl-tRNA synthetase (SerRS): (i) l-serine hydroxamate was utilized by yeast SerRS as a substrate in the ATP-PPi exchange; and (ii) a seryladenylate-like compound was formed from l-serine hydroxamate in the crystal structure of Thermus thermophilus SerRS. To gain clues about the mechanistic difference, we have determined the crystal structures of two complexes of BsLysRS with the adenylate of l-lysine hydroxamate and with 5′-O-[N-(l-Lysyl)sulphamoyl] adenosine. The comparisons of the two BsLysRS structures and the above SerRS structure revealed the specific side-chain shift of Glu411 of BsLysRS in the complex with the adenylate of l-lysine hydroxamate. In support of other structural comparisons, the result suggested that Glu411 plays a key role in the arrangement of PPi for the nucleophilic attack.
机译：氨酰基-tRNA合成酶在氨基酸活化反应中形成酶结合的中间产物氨基酰基烯基化物。通过测量将[ 32 P] PPi掺入ATP的ATP-PPi交换原因来监控该反应。我们以前曾报道过，L-赖氨酸异羟肟酸酯完全抑制了由嗜热脂肪芽孢杆菌（BsLysRS）的赖氨酸-tRNA合成酶催化的L-赖氨酸依赖性ATP-PPi交换反应。几个实验表明，BsLysRS可以使l-赖氨酸异羟肟酸酯发生腺苷酸化，但酶结合的类似lysyladenylate-like化合物不会经历PPi的亲核攻击。这与关于丝氨酰-tRNA合成酶（SerRS）的两个报道形成对照：（i）1-丝氨酸异羟肟酸酯被酵母SerRS用作ATP-PPi交换的底物； （ii）在嗜热菌（Thermus thermophilus）SerRS的晶体结构中，由1-丝氨酸异羟肟酸酯形成类异戊二烯酸酯。为了获得有关机理差异的线索，我们确定了BsLysRS与l-赖氨酸异羟肟酸酯的腺苷酸和5'-O- [N-（l-赖氨酰）磺酰基]腺苷的两种配合物的晶体结构。两种BsLysRS结构和上述SerRS结构的比较揭示了在具有1-赖氨酸异羟肟酸酯的腺苷酸的复合物中，BsLysRS的Glu411的特定侧链移位。为了支持其他结构比较，结果表明Glu411在PPi的亲核攻击排列中起关键作用。

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