Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover.
Amino acid networks in a (β/α)₈ barrel enzyme change during catalytic turnover.
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(β/α)₈ 桶酶中的氨基酸网络在催化周转过程中发生变化。
DOI：
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发表时间：
2014
影响因子：
15
通讯作者：
David D. Boehr
中科院分区：
文献类型：
--
作者：
Jennifer M. Axe;Eric M. Yezdimer;Kathleen F. O’Rourke;Nicole E. Kerstetter;Wanli You;Chia‐en A. Chang;David D. Boehr
蛋白质可以被看作是通过非共价相互作用连接的氨基酸残基的小世界网络。核磁共振化学位移协方差分析用于鉴定色氨酸合酶α亚基中的长程氨基酸网络，包括静息状态（在不存在底物和产物的情况下）和工作状态（在催化转换期间）。观察到的氨基酸网络从蛋白质表面延伸到活性位点，并且在静息状态和工作状态之间是不同的。网络上的表面残基的修饰改变了活性位点残基的结构动力学，并导致催化速率的变化。这些发现表明，氨基酸网络，类似于这里研究的那些，可能是重要的协调酶功能和调节所必需的结构变化。
Proteins can be viewed as small-world networks of amino acid residues connected through noncovalent interactions. Nuclear magnetic resonance chemical shift covariance analyses were used to identify long-range amino acid networks in the α subunit of tryptophan synthase both for the resting state (in the absence of substrate and product) and for the working state (during catalytic turnover). The amino acid networks observed stretch from the surface of the protein into the active site and are different between the resting and working states. Modification of surface residues on the network alters the structural dynamics of active-site residues over 25 Å away and leads to changes in catalytic rates. These findings demonstrate that amino acid networks, similar to those studied here, are likely important for coordinating structural changes necessary for enzyme function and regulation.
基于进化的蛋白质设计。
影响因子：
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作者：
Reynolds,KimberlyA;Russ,WilliamP;Socolich,Michael;Ranganathan,Rama
通讯作者：
Ranganathan,Rama
影响因子：
7.8
作者：
Villali,Janice;Kern,Dorothee
通讯作者：
Kern,Dorothee
DOI：
10.1039/c4cp00110a
发表时间：
2014-04-14
期刊：
Physical chemistry chemical physics : PCCP
影响因子：
--
作者：
Cembran A;Kim J;Gao J;Veglia G
通讯作者：
Veglia G