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A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction
Hu, Cuiyun ; Yu, Caifang ; Liu, Yanhua ; Hou, Xianhui ; Liu, Xiaoyun ; Hu, Yunfei ; Jin, Changwen
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2015
关键词TORSION ANGLE DYNAMICS AUREUS PLASMID PI258 BACILLUS-SUBTILIS PCC 6803 NOE ASSIGNMENT PROTEIN CYANOBACTERIUM DETOXIFICATION PHOSPHATASES RESISTANCE
DOI10.1074/jbc.M115.659896
英文摘要Evolution of enzymes plays a crucial role in obtaining new biological functions for all life forms. Arsenate reductases (ArsC) are several families of arsenic detoxification enzymes that reduce arsenate to arsenite, which can subsequently be extruded from cells by specific transporters. Among these, the Synechocystis ArsC (SynArsC) is structurally homologous to the well characterized thioredoxin (Trx)-coupled ArsC family but requires the glutaredoxin (Grx) system for its reactivation, therefore classified as a unique Trx/Grx-hybrid family. The detailed catalytic mechanism of SynArsC is unclear and how the "hybrid" mechanism evolved remains enigmatic. Herein, we report the molecular mechanism of SynArsC by biochemical and structural studies. Our work demonstrates that arsenate reduction is carried out via an intramolecular thiol-disulfide cascade similar to the Trx-coupled family, whereas the enzyme reactivation step is diverted to the coupling of the glutathione-Grx pathway due to the local structural difference. The current results support the hypothesis that SynArsC is likely a molecular fossil representing an intermediate stage during the evolution of the Trx-coupled ArsC family from the low molecular weight protein phosphotyrosine phosphatase (LMW-PT Pase) family.; National Natural Science Foundation of China [31170681]; SCI(E); EI; PubMed; ARTICLE; yunfei@pku.edu.cn; changwen@pku.edu.cn; 36; 22262-22273; 290
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/416356]  
专题化学与分子工程学院
生命科学学院
推荐引用方式
GB/T 7714
Hu, Cuiyun,Yu, Caifang,Liu, Yanhua,et al. A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2015.
APA Hu, Cuiyun.,Yu, Caifang.,Liu, Yanhua.,Hou, Xianhui.,Liu, Xiaoyun.,...&Jin, Changwen.(2015).A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.JOURNAL OF BIOLOGICAL CHEMISTRY.
MLA Hu, Cuiyun,et al."A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction".JOURNAL OF BIOLOGICAL CHEMISTRY (2015).
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