Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces |
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| Authors: | Kubota Keiko Yamagata Atsushi Sato Yusuke Goto-Ito Sakurako Fukai Shuya |
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| Affiliation: | 1. Department of Nuclear Engineering, Kyoto Univ., Uji, Kyoto 611-0011, Japan;2. Quantum Science and Engineering Center, Kyoto Univ., Uji, Kyoto 611-0011, Japan;3. Department of Electronic Science and Engineering, Kyoto Univ., Nishikyo, Kyoto 615-8510, Japan;4. Laboratory of Cell Biology and Life Science, Graduate School of Human and Environmental Studies, Kyoto Univ., Sakyo, Kyoto 606-8501, Japan;5. CREST, Japan Science and Technology Agency (JST), Chiyoda, Tokyo 102-0075, Japan;1. Nanomaterials Research Group, Integrated Research and Testing Laboratory (LPPT), Gadjah Mada University, Yogyakarta 55281, Indonesia;2. Department of Electrical and Materials Science, Faculty of Engineering Sciences, Kyushu University, Fukuoka 816-8580, Japan;3. Graduate School of Energy of Science, Kyoto University, Kyoto 606-8501, Japan;4. National Institute for Materials Science, Tsukuba, Ibaraki 305-0047, Japan;1. Quantum Science and Engineering Center, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan;2. Department of Physics and Research Center OPTIMAS, University of Kaiserslautern, D-67663 Kaiserslautern, Germany;3. CREST, Japan Science and Technology Agency (JST), Chiyoda, Tokyo 102-0075, Japan;1. Graduate School of Engineering, Hiroshima University, Higashi-Hiroshima, Japan;2. Kyoto University, Gokasho, Uji, Kyoto, Japan;3. JAEA, Naka, Ibaraki, Japan;4. Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan;5. NIFS, Toki, Gifu, Japan;1. Department of Architecture & Architectural Eng. Kyoto University, Kyoto University Katsura Campus, Nishigyo-ku Kyoto-shi, 615-8540, Japan;2. College of Engineering, Hoseo University, Scechul-ri, Baebang-myun, Asan-si, Cuung-nam,336-795, Korea;3. Department of Architecture, Okayama University of Science, Ridaicho, Kita-ku, Okayama-shi,700-0005, Japan |
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| Abstract: | Tail-anchored (TA) proteins are integral membrane proteins that possess a single transmembrane domain near their carboxy terminus. TA proteins play critical roles in many important cellular processes such as membrane trafficking, protein translocation, and apoptosis. The GET complex mediates posttranslational insertion of newly synthesized TA proteins to the endoplasmic reticulum membrane. The GET complex is composed of the homodimeric Get3 ATPase and its heterooligomeric receptor, Get1/2. During insertion, the Get3 dimer shuttles between open and closed conformational states, coupled with ATP hydrolysis and the binding/release of TA proteins. We report crystal structures of ADP-bound Get3 in complex with the cytoplasmic domain of Get1 (Get1CD) in open and semi-open conformations at 3.0‐ and 4.5‐Å resolutions, respectively. Our structures and biochemical data suggest that Get1 uses two interfaces to stabilize the open dimer conformation of Get3. We propose that one interface is sufficient for binding of Get1 by Get3, while the second interface stabilizes the open dimer conformation of Get3. |
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