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-Structure paper
タイトル | Structure of the human plasma membrane Ca-ATPase 1 in complex with its obligatory subunit neuroplastin. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 3623, Year 2018 |
掲載日 | 2018年9月6日 |
![]() | Deshun Gong / Ximin Chi / Kang Ren / Gaoxingyu Huang / Gewei Zhou / Nieng Yan / Jianlin Lei / Qiang Zhou / ![]() ![]() |
PubMed 要旨 | Plasma membrane Ca-ATPases (PMCAs) are key regulators of global Ca homeostasis and local intracellular Ca dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously ...Plasma membrane Ca-ATPases (PMCAs) are key regulators of global Ca homeostasis and local intracellular Ca dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously unrecognized obligatory subunits of PMCAs that dramatically increase the efficiency of PMCA-mediated Ca clearance. Here, we report the cryo-EM structure of human PMCA1 (hPMCA1) in complex with NPTN at a resolution of 4.1 Å for the overall structure and 3.9 Å for the transmembrane domain. The single transmembrane helix of NPTN interacts with the TM-linker and TM10 of hPMCA1. The subunits are required for the hPMCA1 functional activity. The NPTN-bound hPMCA1 closely resembles the E1-Mg structure of endo(sarco)plasmic reticulum Ca ATPase and the Ca site is exposed through a large open cytoplasmic pathway. This structure provides insight into how the subunits bind to the PMCAs and serves as an important basis for understanding the functional mechanisms of this essential calcium pump family. |
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手法 | EM (単粒子) |
解像度 | 4.11 Å |
構造データ | |
化合物 | ![]() ChemComp-NAG: |
由来 |
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![]() | STRUCTURAL PROTEIN / Membrane protein |