7Z17
E. coli C-P lyase bound to a PhnK ABC dimer in an open conformation
Summary for 7Z17
Entry DOI | 10.2210/pdb7z17/pdb |
EMDB information | 14443 |
Descriptor | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI, ... (7 entities in total) |
Functional Keywords | protein complex, transferase, abc, hydrolase, lyase, carbon phosphorus |
Biological source | Escherichia coli More |
Total number of polymer chains | 10 |
Total formula weight | 281419.46 |
Authors | Amstrup, S.K.,Sofos, N.,Karlsen, J.L.,Skjerning, R.B.,Boesen, T.,Enghild, J.J.,Hove-Jensen, B.,Brodersen, D.E. (deposition date: 2022-02-24, release date: 2022-05-25, Last modification date: 2024-07-17) |
Primary citation | Amstrup, S.K.,Ong, S.C.,Sofos, N.,Karlsen, J.L.,Skjerning, R.B.,Boesen, T.,Enghild, J.J.,Hove-Jensen, B.,Brodersen, D.E. Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase. Nat Commun, 14:1001-1001, 2023 Cited by PubMed: 36813778DOI: 10.1038/s41467-023-36604-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.57 Å) |
Structure validation
Download full validation report