8YK5
Structure of glycerophosphoethanolamine ethanolaminephosphodiesterase from Streptomyces sanglieri
Summary for 8YK5
| Entry DOI | 10.2210/pdb8yk5/pdb |
| Descriptor | phospholipase C, CALCIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | phosphodiesterase, long flexible linker, novel c-terminal domain, hydrolase |
| Biological source | Streptomyces sanglieri |
| Total number of polymer chains | 2 |
| Total formula weight | 147956.30 |
| Authors | |
| Primary citation | Murayama, K.,Hosaka, T.,Shirouzu, M.,Sugimori, D. Structure of a phosphodiesterase from Streptomyces sanglieri with a novel C-terminal domain. Biochem.Biophys.Res.Commun., 708:149784-149784, 2024 Cited by PubMed Abstract: A glycerophosphoethanolamine ethanolaminephosphodiesterase (GPE-EP) from Streptomyces sanglieri hydrolyzes glycerophosphoethanolamine to phosphoethanolamine and glycerol. The structure of GPE-EP was determined by the molecular replacement method using a search model generated with AlphaFold2. This structure includes the entire length of the mature protein and it is composed of an N-terminal domain and a novel C-terminal domain connected to a flexible linker. The N-terminal domain is the catalytic domain containing calcium ions at the catalytic site. Coordination bonds were observed between five amino acid residues and glycerol. Although the function of the C-terminal domain is currently unknown, inter-domain interactions between the N- and C-terminal domains may contribute to its relatively high thermostability. PubMed: 38503170DOI: 10.1016/j.bbrc.2024.149784 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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