Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion | |
Xin, Yanlong1,2; Zhao, Yan2; Zheng, Jiangge2; Zhou, Haizhen2; Zhang, Xuejun Cai2,3; Tian, Changlin1,4; Huang, Yihua2,3 | |
刊名 | FASEB JOURNAL |
2018-05-01 | |
卷号 | 32期号:5页码:2411-2421 |
关键词 | X-ray crystallography YidC/Oxa1/Alb3 membrane protein insertase membrane protein biogenesis |
ISSN号 | 0892-6638 |
DOI | 10.1096/fj.201700893RR |
英文摘要 | The evolutionarily conserved YidC/Oxa1/Alb3 family of proteins represents a unique membrane protein family that facilitates the insertion, folding, and assembly of a cohort of alpha-helical membrane proteins in all kingdoms of life, yet its underlying mechanisms remain elusive. We report the crystal structures of the full-length Thermotoga maritima YidC (TmYidC) and the TmYidC periplasmic domain (TmPD) at a resolution of 3.8 and 2.5 angstrom, respectively. The crystal structure of TmPD reveals a beta-supersandwich fold but with apparently shortened beta strands and different connectivity, as compared to the Escherichia coli YidC (EcYidC) periplasmic domain (EcPD). TmYidC in a detergent-solubilized state also adopts a monomeric form and its conserved core domain, which consists of 2 loosely associated alpha-helical bundles, assemble a fold similar to that of the other YidC homologues, yet distinct from that of the archaeal YidC-like DUF106 protein. Functional analysis using in vivo photo-crosslinking experiments demonstrates that Pf3 coat protein, a Sec-independent YidC substrate, exits to the lipid bilayer laterally via one of the 2 alpha-helical bundle interfaces: TM3-TM5. Engineered intramolecular disulfide bonds in TmYidC, in combination with complementation assays, suggest that significant rearrangement of the 2 a-helical bundles at the top of the hydrophilic groove is critical for TmYidC function. These experiments provide a more detailed mechanical insight into YidC-mediated membrane protein biogenesis. |
资助项目 | Ministry of Science and Technology[2016YFA0500404] ; Ministry of Science and Technology[2013CB910603] ; National Natural Science Foundation of China[31625009] ; National Natural Science Foundation of China[31470743] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDB080203] |
WOS关键词 | ESCHERICHIA-COLI YIDC ; PERIPLASMIC DOMAIN ; CRYSTAL-STRUCTURE ; BACTERIAL ; REGIONS ; SECYEG ; TRANSLOCON ; RIBOSOMES ; COMPLEX |
WOS研究方向 | Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology |
语种 | 英语 |
出版者 | FEDERATION AMER SOC EXP BIOL |
WOS记录号 | WOS:000432528000009 |
内容类型 | 期刊论文 |
源URL | [http://ir.hfcas.ac.cn:8080/handle/334002/36563] |
专题 | 合肥物质科学研究院_中科院强磁场科学中心 |
通讯作者 | Tian, Changlin; Huang, Yihua |
作者单位 | 1.Univ Sci & Technol China, Sch Life Sci, Natl Lab Phys Sci Microscale, Hefei, Anhui, Peoples R China 2.Chinese Acad Sci, Ctr Excellence Biomacromoll, Inst Biophys, Natl Lab Biomacromol, Beijing, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China 4.Chinese Acad Sci, High Field Magnet Lab, Hefei, Anhui, Peoples R China |
推荐引用方式 GB/T 7714 | Xin, Yanlong,Zhao, Yan,Zheng, Jiangge,et al. Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion[J]. FASEB JOURNAL,2018,32(5):2411-2421. |
APA | Xin, Yanlong.,Zhao, Yan.,Zheng, Jiangge.,Zhou, Haizhen.,Zhang, Xuejun Cai.,...&Huang, Yihua.(2018).Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion.FASEB JOURNAL,32(5),2411-2421. |
MLA | Xin, Yanlong,et al."Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion".FASEB JOURNAL 32.5(2018):2411-2421. |
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