10BW

Structure of PTDSS2 in complex with POPE

Summary for 10BW

• Entry DOI: 10.2210/pdb10bw/pdb
• EMDB information: 75054
• Descriptor: Phosphatidylserine synthase, O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: phosphatidylserine synthesis, membrane protein
• Biological source: Equus caballus (horse)
• Total number of polymer chains: 2
• Total formula weight: 123162.61

Authors

Lie, W.,Ming, Z. (deposition date: 2026-01-11, release date: 2026-10-28)

Primary citation

Wang, L.,Zhang, Z.,Yang, H.,Laganowsky, A.,Zhou, M.
Mechanisms of substrate recognition and catalysis in a mammalian phosphatidylserine synthase 2.
Proc.Natl.Acad.Sci.USA, 123:e2607382123-e2607382123, 2026

PubMed Abstract: Mammalian phosphatidylserine synthase-1 and -2, PSS1 and PSS2, synthesize phosphatidylserine (PS) by replacing the headgroup of either phosphatidylcholine or phosphatidylethanolamine (PE) with a serine. We determined structures of PSS2 from in complex with either a PE or a serine substrate to resolutions of 2.8 to 3.2 Å. The structures define substrate binding sites and reveal that the phosphate group of the PE is coordinated by two Ca. In addition, we found that PSS2 has significant phospholipase D (PLD) activity in the absence of serine and that Ca is required for the PLD activity. These findings enrich and refine our knowledge in the mechanisms of substrate recognition and catalysis in mammalian PSS.

PubMed: 42809401
DOI: 10.1073/pnas.2607382123

Experimental method

ELECTRON MICROSCOPY (3.2 Å)