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TitleConformational cycle of human polyamine transporter ATP13A2.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 1978, Year 2023
Publish dateApr 8, 2023
AuthorsJianqiang Mu / Chenyang Xue / Lei Fu / Zongjun Yu / Minhan Nie / Mengqi Wu / Xinmeng Chen / Kun Liu / Ruiqian Bu / Ying Huang / Baisheng Yang / Jianming Han / Qianru Jiang / Kevin C Chan / Ruhong Zhou / Huilin Li / Ancheng Huang / Yong Wang / Zhongmin Liu /
PubMed AbstractDysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a ...Dysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a transporter with a critical role in balancing the polyamine concentration between the lysosome and the cytosol. Here, to better understand human ATP13A2-mediated polyamine transport, we use single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2 in six intermediate states, including the putative E2 structure for the P5 subfamily of the P-type ATPases. These structures comprise a nearly complete conformational cycle spanning the polyamine transport process and capture multiple substrate binding sites distributed along the transmembrane regions, suggesting a potential polyamine transport pathway. Integration of high-resolution structures, biochemical assays, and molecular dynamics simulations allows us to obtain a better understanding of the structural basis of how hATP13A2 transports polyamines, providing a mechanistic framework for ATP13A2-related diseases.
External linksNat Commun / PubMed:37031211 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 5.65 Å
Structure data

EMDB-35384, PDB-8iek:
Cryo-EM structure of ATP13A2 in the E1-ATP state
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-35385, PDB-8iel:
Cryo-EM structure of ATP13A2 in the E1-like state
Method: EM (single particle) / Resolution: 5.65 Å

EMDB-35386, PDB-8iem:
Cryo-EM structure of ATP13A2 in the E2P state
Method: EM (single particle) / Resolution: 3.35 Å

EMDB-35387, PDB-8ien:
Cryo-EM structure of ATP13A2 in the E2-Pi state
Method: EM (single particle) / Resolution: 3.25 Å

EMDB-35388, PDB-8ieo:
Cryo-EM structure of ATP13A2 in the nominal E1P state
Method: EM (single particle) / Resolution: 3.78 Å

EMDB-35391, PDB-8ier:
Cryo-EM structure of ATP13A2 in the putative of E2 state
Method: EM (single particle) / Resolution: 4.87 Å

EMDB-35392, PDB-8ies:
Cryo-EM structure of ATP13A2 in the E1P-ADP state
Method: EM (single particle) / Resolution: 3.73 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-SPM:
SPERMINE

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / Cryo-EM structure of ATP13A2 in the E1-ATP state; Membran protein / Cryo-EM structure of ATP13A2 in the E1-like state / membrane protein / Cryo-EM structure of ATP13A2 in the E2P state; Membran protein / TRANSPORT PROTEIN / Cryo-EM structure of ATP13A2 in the E2-Pi state / Cryo-EM structure of ATP13A2 in the nominal E1P state; Membrane protein / Cryo-EM structure of ATP13A2 in the putative of E2 state; Membrane protein / Cryo-EM structure of ATP13A2 in the E1P-ADP state; Membrane protein

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