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8J2M

The truncated rice Na+/H+ antiporter SOS1 (1-976) in a constitutively active state

Summary for 8J2M
Entry DOI10.2210/pdb8j2m/pdb
Related8IWO
EMDB information35775 35950
DescriptorNa+/H+ antiporter, (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl tetradecanoate (2 entities in total)
Functional Keywordsna+/h+ antiporter, cation:proton antiporter family 1, membrane protein
Biological sourceOryza sativa Japonica Group (Japanese rice)
Total number of polymer chains2
Total formula weight234392.80
Authors
Zhang, X.Y.,Tang, L.H.,Zhang, C.R.,Nie, J.W.,Chen, Y.H. (deposition date: 2023-04-14, release date: 2023-11-22, Last modification date: 2024-11-13)
Primary citationZhang, X.Y.,Tang, L.H.,Nie, J.W.,Zhang, C.R.,Han, X.,Li, Q.Y.,Qin, L.,Wang, M.H.,Huang, X.,Yu, F.,Su, M.,Wang, Y.,Xu, R.M.,Guo, Y.,Xie, Q.,Chen, Y.H.
Structure and activation mechanism of the rice Salt Overly Sensitive 1 (SOS1) Na + /H + antiporter.
Nat.Plants, 9:1924-1936, 2023
Cited by
PubMed Abstract: Salinity is one of the most severe abiotic stresses that adversely affect plant growth and agricultural productivity. The plant Na/H antiporter Salt Overly Sensitive 1 (SOS1) located in the plasma membrane extrudes excess Na out of cells in response to salt stress and confers salt tolerance. However, the molecular mechanism underlying SOS1 activation remains largely elusive. Here we elucidate two cryo-electron microscopy structures of rice (Oryza sativa) SOS1, a full-length protein in an auto-inhibited state and a truncated version in an active state. The SOS1 forms a dimeric architecture, with an NhaA-folded transmembrane domain portion in the membrane and an elongated cytosolic portion of multiple regulatory domains in the cytoplasm. The structural comparison shows that SOS1 adopts an elevator transport mechanism accompanied by a conformational transition of the highly conserved Pro in the unwound transmembrane helix 5 (TM), switching from an occluded conformation in the auto-inhibited state to a conducting conformation in the active state. These findings allow us to propose an inhibition-release mechanism for SOS1 activation and elucidate how SOS1 controls Na homeostasis in response to salt stress.
PubMed: 37884653
DOI: 10.1038/s41477-023-01551-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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数据于2025-07-16公开中

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