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-Structure paper
| タイトル | Structure of the [Ca]E2P intermediate of Ca-ATPase 1 from Listeria monocytogenes. |
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| ジャーナル・号・ページ | EMBO Rep, Vol. 26, Issue 7, Page 1709-1723, Year 2025 |
| 掲載日 | 2025年2月27日 |
著者 | Sara Basse Hansen / Rasmus Kock Flygaard / Magnus Kjaergaard / Poul Nissen / ![]() |
| PubMed 要旨 | Active transport by P-type Ca-ATPases maintain internal calcium stores and a low cytosolic calcium concentration. Structural studies of mammalian sarco/endoplasmic reticulum Ca-ATPases (SERCA) have ...Active transport by P-type Ca-ATPases maintain internal calcium stores and a low cytosolic calcium concentration. Structural studies of mammalian sarco/endoplasmic reticulum Ca-ATPases (SERCA) have revealed several steps of the transport cycle, but a calcium-releasing intermediate has remained elusive. Single-molecule FRET studies of the bacterial Ca-ATPase LMCA1 revealed an intermediate of the transition between so-called [Ca]E1P and E2P states and suggested that calcium release from this intermediate was the essentially irreversible step of transport. Here, we present a 3.5 Å resolution cryo-EM structure for a four-glycine insertion mutant of LMCA1 in a lipid nanodisc obtained under conditions with calcium and ATP and adopting such an intermediate state, denoted [Ca]E2P. The cytosolic domains are positioned in the E2P-like conformation, while the calcium-binding transmembrane (TM) domain adopts a calcium-bound E1P-ADP-like conformation. Missing density for the E292 residue at the calcium site (the equivalent of SERCA1a E309) suggests flexibility and a site poised for calcium release and proton uptake. The structure suggests a mechanism where ADP release and re-organization of the cytoplasmic domains precede calcium release. |
リンク | EMBO Rep / PubMed:40016426 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.46 Å |
| 構造データ | EMDB-51510, PDB-9gqo: |
| 化合物 | ![]() ChemComp-CA: ![]() ChemComp-MG: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / Intermediate / P-type ATPase / Calcium Transport |
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listeria monocytogenes (バクテリア)
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