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7Z18

E. coli C-P lyase bound to a PhnK ABC dimer and ATP

Summary for 7Z18
Entry DOI10.2210/pdb7z18/pdb
EMDB information14444
DescriptorAlpha-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, ... (10 entities in total)
Functional Keywordsprotein complex, transferase, abc, hydrolase, lyase, carbon phosphorus
Biological sourceEscherichia coli
More
Total number of polymer chains10
Total formula weight282774.51
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 citationAmstrup, 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 (1.98 Å)
Structure validation

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