Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step

文献类型： 外文期刊

第一作者： Zhang, Han

作者： Zhang, Han;Li, Yuchen;Nie, Jinglei;Ren, Jie;Zeng, An-Ping;Ren, Jie;Zeng, An-Ping

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期刊名称：COMMUNICATIONS BIOLOGY （ 影响因子：6.268； 五年影响因子：6.268 ）

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年卷期： 2020 年 3 卷 1 期

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收录情况： SCI

摘要： Molecular shuttles play decisive roles in many multi-enzyme systems such as the glycine cleavage system (GCS) for one-carbon (C1) metabolism. In GCS, a lipoate swinging arm containing an aminomethyl moiety is attached to protein H and serves as a molecular shuttle among different proteins. Protection of the aminomethyl moiety in a cavity of protein H and its release induced by protein T are key processes but barely understood. Here, we present a detailed structure-based dynamic analysis of the induced release of the lipoate arm of protein H. Based on molecular dynamics simulations of interactions between proteins H and T, four major steps of the release process showing significantly different energy barriers and time scales can be distinguished. Mutations of a key residue, Ser-67 in protein H, led to a bidirectional tuning of the release process. This work opens ways to target C1 metabolism in biomedicine and the utilization of formate and CO2 for biosynthesis. Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase the overall reaction rate of glycine cleavage by more than twice, providing a strategy for manipulating this reaction system for use in synthetic biology.

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