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TitleStructural basis of the P4B ATPase lipid flippase activity.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 5963, Year 2021
Publish dateOct 13, 2021
AuthorsLin Bai / Bhawik K Jain / Qinglong You / H Diessel Duan / Mehmet Takar / Todd R Graham / Huilin Li /
PubMed AbstractP4 ATPases are lipid flippases that are phylogenetically grouped into P4A, P4B and P4C clades. The P4A ATPases are heterodimers composed of a catalytic α-subunit and accessory β-subunit, and the ...P4 ATPases are lipid flippases that are phylogenetically grouped into P4A, P4B and P4C clades. The P4A ATPases are heterodimers composed of a catalytic α-subunit and accessory β-subunit, and the structures of several heterodimeric flippases have been reported. The S. cerevisiae Neo1 and its orthologs represent the P4B ATPases, which function as monomeric flippases without a β-subunit. It has been unclear whether monomeric flippases retain the architecture and transport mechanism of the dimeric flippases. Here we report the structure of a P4B ATPase, Neo1, in its E1-ATP, E2P-transition, and E2P states. The structure reveals a conserved architecture as well as highly similar functional intermediate states relative to dimeric flippases. Consistently, structure-guided mutagenesis of residues in the proposed substrate translocation path disrupted Neo1's ability to establish membrane asymmetry. These observations indicate that evolutionarily distant P4 ATPases use a structurally conserved mechanism for substrate transport.
External linksNat Commun / PubMed:34645814 / PubMed Central
MethodsEM (single particle)
Resolution3.08 - 5.64 Å
Structure data

24413

7rd6

EMDB-24413, PDB-7rd6:
Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P state
Method: EM (single particle) / Resolution: 3.25 Å

24414

7rd7

EMDB-24414, PDB-7rd7:
Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P-transition state
Method: EM (single particle) / Resolution: 3.08 Å

24415

7rd8

EMDB-24415, PDB-7rd8:
Structure of the S. cerevisiae P4B ATPase lipid flippase in the E1-ATP state
Method: EM (single particle) / Resolution: 5.64 Å

Chemicals

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-MG:
Unknown entry

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSLOCASE / P4B ATPase lipid flippase

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