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Structure paper

TitleCryo-EM structures and transport mechanism of human P5B type ATPase ATP13A2.
Journal, issue, pagesCell Discov, Vol. 7, Issue 1, Page 106, Year 2021
Publish dateNov 2, 2021
AuthorsXudong Chen / Mingze Zhou / Sensen Zhang / Jian Yin / Ping Zhang / Xujun Xuan / Peiyi Wang / Zhiqiang Liu / Boda Zhou / Maojun Yang /
PubMed AbstractPolyamines are important polycations that play critical roles in mammalian cells. ATP13A2 belongs to the orphan P5B adenosine triphosphatases (ATPase) family and has been established as a lysosomal ...Polyamines are important polycations that play critical roles in mammalian cells. ATP13A2 belongs to the orphan P5B adenosine triphosphatases (ATPase) family and has been established as a lysosomal polyamine exporter to maintain the normal function of lysosomes and mitochondria. Previous studies have reported that several human neurodegenerative disorders are related to mutations in the ATP13A2 gene. However, the transport mechanism of ATP13A2 in the lysosome remains unclear. Here, we report the cryo-electron microscopy (cryo-EM) structures of three distinct intermediates of the human ATP13A2, revealing key insights into the spermine (SPM) transport cycle in the lysosome. The transmembrane domain serves as a substrate binding site and the C-terminal domain is essential for protein stability and may play a regulatory role. These findings advance our understanding of the polyamine transport mechanism, the lipid-associated regulation, and the disease-associated mutants of ATP13A2.
External linksCell Discov / PubMed:34728622 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 3.6 Å
Structure data

31623

7fjm

EMDB-31623, PDB-7fjm:
Cryo EM structure of lysosomal ATPase
Method: EM (single particle) / Resolution: 3.3 Å

31626

7fjp

EMDB-31626, PDB-7fjp:
Cryo EM structure of lysosomal ATPase
Method: EM (single particle) / Resolution: 3.0 Å

31627

7fjq

EMDB-31627, PDB-7fjq:
Cryo EM structure of lysosomal ATPase
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION / Phosphate

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

ChemComp-MG:
Unknown entry

ChemComp-SPM:
SPERMINE / Spermine

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / lysosomal ATPase transporter

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