8YR5
Crystal structure of E. coli phosphatidylserine synthase in apo state
Summary for 8YR5
| Entry DOI | 10.2210/pdb8yr5/pdb |
| Related | 8YR6 |
| Descriptor | CDP-diacylglycerol--serine O-phosphatidyltransferase, SULFATE ION (2 entities in total) |
| Functional Keywords | apo, phospholipid metabolism, peripheral membrane protein, phosphatidylserine, membrane protein, transferase |
| Biological source | Escherichia coli str. K-12 substr. MG1655 |
| Total number of polymer chains | 12 |
| Total formula weight | 650291.69 |
| Authors | |
| Primary citation | Lee, E.,Cho, G.,Kim, J. Structural basis for membrane association and catalysis by phosphatidylserine synthase in Escherichia coli. Sci Adv, 10:eadq4624-eadq4624, 2024 Cited by PubMed Abstract: Phosphatidylserine synthase (PssA) is essential in the biosynthesis of phosphatidylethanolamine, a major phospholipid of bacterial membranes. A peripheral membrane protein PssA can associate with the cellular membrane in its active state or exist in the cytosol in an inactive form. The membrane-bound enzyme acts on cytidine diphosphate diacylglycerol (CDP-DG) to form cytidine monophosphate and a covalent intermediate, which is subsequently targeted by serine to produce phosphatidylserine. Here, we present two crystal structures of PssA, one complexed with CDP-DG and the other without. The lipid-bound structure mimics the Michaelis complex before the formation of a covalent intermediate, revealing key determinants for substrate recognition and catalysis. Notably, membrane-free PssA is in a monomer-dimer equilibrium, with only the monomer capable of associating with the membrane, suggesting a regulatory mechanism for phospholipid biosynthesis dependent on the oligomerization state of the enzyme. PubMed: 39693441DOI: 10.1126/sciadv.adq4624 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.83 Å) |
Structure validation
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