Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase.

Effects of Distal Mutations on Prolyl-Adenylate Formation of Escherichia coli Prolyl-tRNA Synthetase.
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DOI:
10.1007/s10930-020-09910-3
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发表时间:
2020-10
期刊:
The protein journal
影响因子:
--
通讯作者:
Hati S
Hati S
中科院分区:
其他
文献类型:
--
作者:
Zajac J;Anderson H;Adams L;Wangmo D;Suhail S;Almen A;Berns L;Coerber B;Dawson L;Hunger A;Jehn J;Johnson J;Plack N;Strasser S;Williams M;Bhattacharyya S;Hati S

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Enzymes play important roles in many biological processes. Amino acid residues in the active site pocket of an enzyme, which are in direct contact with the substrate(s), are generally believed to be critical for substrate recognition and catalysis. Identifying and understanding how these “catalytic” residues help enzymes achieve enormous rate enhancement has been the focus of many structural and biochemical studies over the past several decades. Recent studies have shown that enzymes are intrinsically dynamic and dynamic coupling between distant structural elements is essential for effective catalysis in modular enzymes. Therefore, distal residues are expected to have impacts on enzyme function. However, few studies have investigated the role of distal residues on enzymatic catalysis. In the present study, effects of distal residue mutations on the catalytic function of an aminoacyl-tRNA synthetase, namely, prolyl-tRNA synthase, were investigated. The present study demonstrates that distal residues significantly contribute to catalysis of the modular Escherichia coli prolyl-tRNA synthetase by maintaining intrinsic protein flexibility.
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