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: 2023-03-08)

• 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; PubMed: 36813778; DOI: 10.1038/s41467-023-36604-y

Experimental method

ELECTRON MICROSCOPY (2.57 Å)