7Z16

E. coli C-P lyase bound to PhnK/PhnL dual ABC dimer with AMPPNP and PhnK E171Q mutation

Summary for 7Z16

Entry DOI	10.2210/pdb7z16/pdb
EMDB information	14442
Descriptor	Phosphonate C-P lyase system protein PhnG, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH, ... (11 entities in total)
Functional Keywords	protein complex, transferase, abc, hydrolase, lyase, carbon-phosphorus, sam
Biological source	Escherichia coli More
Total number of polymer chains	12
Total formula weight	331851.29
Authors	Amstrup, S.K.,Sofus, 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: 2022-06-22, 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 Cited by PubMed: 36813778 DOI: 10.1038/s41467-023-36604-y PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (2.09 Å)

Structure validation