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-Structure paper
タイトル | The structure and function of P5A-ATPases. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 9605, Year 2024 |
掲載日 | 2024年11月6日 |
![]() | Ping Li / Viktoria Bågenholm / Per Hägglund / Karin Lindkvist-Petersson / Kaituo Wang / Pontus Gourdon / ![]() ![]() ![]() |
PubMed 要旨 | Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of ...Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of a P5A-ATPase, CtSpf1, covering multiple transport intermediates of the E1 → E1-ATP → E1P-ADP → E1P → E2P → E2.P → E2 → E1 cycle. In the E2P and E2.P states a cleft spans the entire membrane, holding a polypeptide cargo molecule. The cargo includes an ER luminal extension, pinpointed as the C-terminus in the E2.P state, which reenters the membrane in E2P. The E1 structure harbors a cytosol-facing cavity that is blocked by an insertion we refer to as the Plug-domain. The Plug-domain is nestled to key ATPase features and is displaced in the E1P-ADP and E1P states. Collectively, our findings are compatible with a broad range of proteins as cargo, with the P5A-ATPases serving a role in membrane removal of helices, although insertion/secretion cannot be excluded, as well as with a mechanistic role of the Plug-domain. |
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手法 | EM (単粒子) |
解像度 | 3.2 - 3.79 Å |
構造データ | EMDB-17039, PDB-8op3: EMDB-17040, PDB-8op4: EMDB-17041, PDB-8op5: EMDB-17042, PDB-8op6: EMDB-17043, PDB-8op7: EMDB-17044, PDB-8op8: |
化合物 | ![]() ChemComp-ANP: ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-ALF: ![]() ChemComp-HOH: ![]() ChemComp-BEF: ![]() ChemComp-CA: |
由来 |
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![]() | MEMBRANE PROTEIN / translocase |