7CNY
Crystal structure of 8PE bound PSD from E. coli (2.12 A)
Summary for 7CNY
| Entry DOI | 10.2210/pdb7cny/pdb |
| Descriptor | Phosphatidylserine decarboxylase beta chain, Phosphatidylserine decarboxylase alpha chain, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total) |
| Functional Keywords | phosphatidylserine decarboxylase, pyruvoyl-dependent decarboxylase, auto-cleaved, serine protease, product bound, 8:0/8:0 pe, 8:0/8:0 phosphatidylethanolamine, 8:0 pe, schiff base reduction by nacnbh3, membrane protein, lyase |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 4 |
| Total formula weight | 68210.76 |
| Authors | |
| Primary citation | Cho, G.,Lee, E.,Kim, J. Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis. Sci Rep, 11:5785-5785, 2021 Cited by PubMed Abstract: Phosphatidylethanolamine (PE), a major component of the cellular membrane across all domains of life, is synthesized exclusively by membrane-anchored phosphatidylserine decarboxylase (PSD) in most bacteria. The enzyme undergoes auto-cleavage for activation and utilizes the pyruvoyl moiety to form a Schiff base intermediate with PS to facilitate decarboxylation. However, the structural basis for self-maturation, PS binding, and decarboxylation processes directed by PSD remain unclear. Here, we present X-ray crystal structures of PSD from Escherichia coli, representing an apo form and a PE-bound complex, in which the phospholipid is chemically conjugated to the essential pyruvoyl residue, mimicking the Schiff base intermediate. The high-resolution structures of PE-complexed PSD clearly illustrate extensive hydrophobic interactions with the fatty acyl chains of the phospholipid, providing insights into the broad specificity of the enzyme over a wide range of cellular PS. Furthermore, these structures strongly advocate the unique topology of the enzyme in a lipid bilayer environment, where the enzyme associates with cell membranes in a monotopic fashion via the N-terminal domain composed of three amphipathic helices. Lastly, mutagenesis analyses reveal that E. coli PSD primarily employs D90/D142-H144-S254 to achieve auto-cleavage for the proenzyme maturation, where D90 and D142 act in complementary to each other. PubMed: 33707636DOI: 10.1038/s41598-021-85195-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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