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Structure paper

TitleStructural basis for catalytic mechanism of human phosphatidylserine synthase 1.
Journal, issue, pagesCell Discov, Vol. 11, Issue 1, Page 20, Year 2025
Publish dateMar 6, 2025
AuthorsYingjie Ning / Ruisheng Xu / Jie Yu / Jingpeng Ge /
External linksCell Discov / PubMed:40044636 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.25 Å
Structure data

62503

9kqf

EMDB-62503, PDB-9kqf:
Cryo-EM structure of PSS1 in the absence of calcium or L-serine
Method: EM (single particle) / Resolution: 3.25 Å

62505

9kqi

EMDB-62505, PDB-9kqi:
Cryo-EM structure of PSS1 with calcium and L-serine
Method: EM (single particle) / Resolution: 3.02 Å

62506

9kqj

EMDB-62506, PDB-9kqj:
Cryo-EM structure of PSS1 with calcium
Method: EM (single particle) / Resolution: 2.95 Å

Chemicals

ChemComp-PSF:
1,2-DICAPROYL-SN-PHOSPHATIDYL-L-SERINE

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-D12:
DODECANE

ChemComp-C14:
TETRADECANE

ChemComp-T7X:
Phosphatidylinositol

ChemComp-CA:
Unknown entry

ChemComp-SER:
SERINE

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / phosphatidylserine synthase / ER membrane protein / integral membrane protein / transmembrane enzyme / PS

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