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-Structure paper
| タイトル | Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. |
|---|---|
| ジャーナル・号・ページ | Science, Vol. 360, Issue 6385, Page 215-219, Year 2018 |
| 掲載日 | 2018年4月13日 |
著者 | Katharina Braunger / Stefan Pfeffer / Shiteshu Shrimal / Reid Gilmore / Otto Berninghausen / Elisabet C Mandon / Thomas Becker / Friedrich Förster / Roland Beckmann / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Science / PubMed:29519914 / PubMed Central |
| 手法 | EM (サブトモグラム平均) / EM (単粒子) |
| 解像度 | 4.2 - 30.0 Å |
| 構造データ | ![]() EMDB-4306: ![]() EMDB-4307: ![]() EMDB-4308: ![]() EMDB-4309: ![]() EMDB-4310: ![]() EMDB-4311: ![]() EMDB-4312: ![]() EMDB-4313: ![]() EMDB-4314: EMDB-4315, PDB-6ftg: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-ZN: ![]() ChemComp-9UB: |
| 由来 |
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キーワード | PROTEIN TRANSPORT / Protein translocon of the endoplasmic reticulum |
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