THE USE OF DOUBLE MUTANTS TO DETECT STRUCTURAL-CHANGES IN THE ACTIVE-SITE OF THE TYROSYL-TRANSFER RNA-SYNTHETASE (BACILLUS-STEAROTHERMOPHILUS)
THE USE OF DOUBLE MUTANTS TO DETECT STRUCTURAL-CHANGES IN THE ACTIVE-SITE OF THE TYROSYL-TRANSFER RNA-SYNTHETASE (BACILLUS-STEAROTHERMOPHILUS)
复制标题
DOI：
10.1016/0092-8674(84)90278-2
复制
发表时间：
1984-01-01
期刊：
影响因子：
64.5
通讯作者：
FERSHT, AR
中科院分区：
文献类型：
--
作者：
CARTER, PJ;WINTER, G;FERSHT, AR
在以前的研究中，酪氨酸-tRNA合成酶的突变体，其中苏氨酸残基（Thr 51）转化为脯氨酸显着提高了酶的ATP底物的亲和力。Pro51如何提高酶对ATP的亲和力？先验地，Pro51可能直接与ATP相互作用，或者它可能扭曲多肽骨架并迫使酶与ATP的其他地方产生新的或改善的接触。通过在2个残基处制造Pro 51酶的突变体，使H与ATP底物形成键合，结果表明Pro 51大大提高了其中1个接触的强度。通过引入进一步的突变，可以检测由突变诱导的酶中结构变化的传播。
In a previous study, a mutant of tyrosyl-tRNA synthetase in which a threonine residue (Thr51) was converted to proline dramatically improved the affinity of the enzyme for its ATP substrate. How does Pro51 improve the enzyme''s affinity for ATP? A priori, Pro51 might interact directly with the ATP or it might distort the polypeptide backbone and force new or improved contacts elsewhere from the enzyme to ATP. By making mutants of the Pro51 enyzme at 2 residues that make H bonds to the ATP substrate, it was shown that Pro51 greatly improves the strength of 1 of these contacts. The propagation of a structural change in an enzyme induced by mutation may be detected by the introduction of further mutations.