Journal
STRUCTURE
Volume 24, Issue 1, Pages 37-42Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.11.009
Keywords
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Funding
- NIH [GM103917]
- Department of Biochemistry and Biophysics
- Center for Phage Technology at Texas AM University
- Welch Foundation [A-1863]
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The carbon-phosphorus (C-P) lyase complex is essential for the metabolism of unactivated phosphonates to phosphate in bacteria. Using single-particle cryo-electron microscopy, we determined two structures of the C-P lyase core complex PhnG(2)H(2)I(2)J(2), with or without PhnK. PhnG(2)H(2)I(2)J(2) is a two-fold symmetric hetero-octamer. Its two PhnJ subunits provide two identical binding sites for PhnK. Only one PhnK binds to PhnG(2)H(2)I(2)J(2) due to steric hindrance. PhnK is homologous to the nucleotide-binding domain (NBD) of ATP-binding cassette transporters. The a helices 3 and 4 of PhnK bind to a helix 6 and a loop (residues 227-230) of PhnJ, in a different mode from the binding of NBDs to their transmembrane partners. Moreover, binding of PhnK exposes the active site residue, Gly32 of PhnJ, located near the interface between PhnJ and PhnH. This structural information provides a basis for further deciphering of the reaction mechanism of the C-P lyase.
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