Structure of an EIIC sugar transporter trapped in an inward-facing conformation
文献类型:期刊论文
作者 | Yin Nian2,3; Zhichun Xu2,3; Ming Zhou2,3; Wonpil Im4; Allan Chris M. Ferreon1; Mahdi Muhammad Moosa1; Liya Hu2; Jason G. McCoy2; Zhenning Ren2; Jumin Lee4 |
刊名 | PNAS |
出版日期 | 2018 |
卷号 | 115期号:23页码:5962–5967 |
关键词 | Bcmalt Double-cysteine Cross-linking Inward-facing Conformation Single-molecule Fret Elevator-type Mechanism Of Transport |
DOI | 10.1073/pnas.1800647115 |
英文摘要 | The phosphoenolpyruvate-dependent phosphotransferase system(PTS) transports sugar into bacteria and phosphorylates the sugarfor metabolic consumption. The PTS is important for the survival ofbacteria and thus a potential target for antibiotics, but itsmechanism of sugar uptake and phosphorylation remains unclear.The PTS is composed of multiple proteins, and the membrane-embedded Enzyme IIC (EIIC) component transports sugars acrossthe membrane. Crystal structures of two members of the glucosesuperfamily of EIICs, bcChbC and bcMalT, were solved in the inward-facing and outward-facing conformations, and the structures sug-gest that sugar translocation could be achieved by movement ofa structured domain that contains the sugar-binding site. How-ever, different conformations have not been captured on thesame transporter to allow precise description of the conforma-tional changes. Here we present a crystal structure of bcMalT trap-ped in an inward-facing conformation by a mercury ion thatbridges two strategically placed cysteine residues. The structureallows direct comparison of the outward- and inward-facing con-formations and reveals a large rigid-body motion of the sugar-binding domain and other conformational changes that accompanythe rigid-body motion. All-atom molecular dynamics simulationsshow that the inward-facing structure is stable with or withoutthe cross-linking. The conformational changes were further val-idated by single-molecule Föster resonance energy transfer(smFRET). Combined, these results establish the elevator-typemechanism of transport in the glucose superfamily of EIICtransporters. |
语种 | 英语 |
源URL | [http://159.226.149.26:8080/handle/152453/12326] |
专题 | 昆明动物研究所_离子通道药物研发中心 |
作者单位 | 1.Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030 2.Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030 3.Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China 4.Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015 |
推荐引用方式 GB/T 7714 | Yin Nian,Zhichun Xu,Ming Zhou,et al. Structure of an EIIC sugar transporter trapped in an inward-facing conformation[J]. PNAS,2018,115(23):5962–5967. |
APA | Yin Nian.,Zhichun Xu.,Ming Zhou.,Wonpil Im.,Allan Chris M. Ferreon.,...&Jumin Lee.(2018).Structure of an EIIC sugar transporter trapped in an inward-facing conformation.PNAS,115(23),5962–5967. |
MLA | Yin Nian,et al."Structure of an EIIC sugar transporter trapped in an inward-facing conformation".PNAS 115.23(2018):5962–5967. |
入库方式: OAI收割
来源:昆明动物研究所
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