Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Academic Article

abstract

• 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 PhnG2H2I2J2, with or without PhnK. PhnG2H2I2J2 is a two-fold symmetric hetero-octamer. Its two PhnJ subunits provide two identical binding sites for PhnK. Only one PhnK binds to PhnG2H2I2J2 due to steric hindrance. PhnK is homologous to the nucleotide-binding domain (NBD) of ATP-binding cassette transporters. The helices 3 and 4 of PhnK bind to 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.

authors

• Raushel, Frank
• Zhang, Junjie

published proceedings

• Structure

author list (cited authors)

• Yang, K., Ren, Z., Raushel, F. M., & Zhang, J.

citation count

• 13

complete list of authors

• Yang, Kailu||Ren, Zhongjie||Raushel, Frank M||Zhang, Junjie

publication date

• January 2016

publisher

• Elsevier  Publisher

published in

• Structure  Journal

keywords

• Adenosine Triphosphate
• Amino Acid Sequence
• Binding Sites
• Escherichia Coli
• Escherichia Coli Proteins
• Lyases
• Molecular Sequence Data
• Protein Binding

PubMed Central ID

• 26724995

Digital Object Identifier (DOI)

• 10.1016/j.str.2015.11.009

start page

• 37

end page

• 42

volume

• 24

issue

• 1

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.str.2015.11.009