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DOI | 10.1126/science.aar7899 |
Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum | |
Braunger, Katharina1,2; Pfeffer, Stefan3; Shrimal, Shiteshu4; Gilmore, Reid4; Berninghausen, Otto1,2; Mandon, Elisabet C.4; Becker, Thomas1,2; Foerster, Friedrich5; Beckmann, Roland1,2 | |
2018-04-13 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2018 |
卷号 | 360期号:6385页码:215-218 |
文章类型 | Article |
语种 | 英语 |
国家 | Germany; USA; Netherlands |
英文摘要 | Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo-electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000429805400049 |
WOS关键词 | BACTERIAL OLIGOSACCHARYLTRANSFERASE ; RIBOSOME-SEC61 COMPLEX ; MOLECULAR-BASIS ; MEMBRANE ; TRANSLOCATION ; POLYPEPTIDES ; INSERTION ; ISOFORMS ; INSIGHTS ; CHANNEL |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/198402 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Munich, Gene Ctr, Dept Biochem, D-81377 Munich, Germany; 2.Univ Munich, Ctr Integrated Prot Sci Munich, D-81377 Munich, Germany; 3.Max Planck Inst Biochem, Dept Mol Struct Biol, D-82152 Martinsried, Germany; 4.Univ Massachusetts, Med Sch, Dept Biochem & Mol Pharmacol, Worcester, MA 01605 USA; 5.Univ Utrecht, Bijvoet Ctr Biomol Res, Cryoelectron Microscopy, NL-3584 CH Utrecht, Netherlands |
推荐引用方式 GB/T 7714 | Braunger, Katharina,Pfeffer, Stefan,Shrimal, Shiteshu,et al. Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum[J]. SCIENCE,2018,360(6385):215-218. |
APA | Braunger, Katharina.,Pfeffer, Stefan.,Shrimal, Shiteshu.,Gilmore, Reid.,Berninghausen, Otto.,...&Beckmann, Roland.(2018).Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum.SCIENCE,360(6385),215-218. |
MLA | Braunger, Katharina,et al."Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum".SCIENCE 360.6385(2018):215-218. |
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