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Cryo-EM structure of a P-type ATPaseCryo-EM structure of a P-type ATPase
Structural highlights
FunctionAT2B1_HUMAN This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. Publication Abstract from PubMedPlasma membrane Ca(2+)-ATPases (PMCAs) are key regulators of global Ca(2+) homeostasis and local intracellular Ca(2+) dynamics. Recently, Neuroplastin (NPTN) and basigin were identified as previously unrecognized obligatory subunits of PMCAs that dramatically increase the efficiency of PMCA-mediated Ca(2+) clearance. Here, we report the cryo-EM structure of human PMCA1 (hPMCA1) in complex with NPTN at a resolution of 4.1 A for the overall structure and 3.9 A for the transmembrane domain. The single transmembrane helix of NPTN interacts with the TM8-9-linker and TM10 of hPMCA1. The subunits are required for the hPMCA1 functional activity. The NPTN-bound hPMCA1 closely resembles the E1-Mg(2+) structure of endo(sarco)plasmic reticulum Ca(2+) ATPase and the Ca(2+) 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. Structure of the human plasma membrane Ca(2+)-ATPase 1 in complex with its obligatory subunit neuroplastin.,Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, Zhou Q Nat Commun. 2018 Sep 6;9(1):3623. doi: 10.1038/s41467-018-06075-7. PMID:30190470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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