title: (1)H, (13)C and (15)N backbone and side-chain resonance assignments of reduced CcmG from Escherichia coli.
abstract: CcmG is a periplasmic, membrane-anchored protein widely distributed in a variety of species. In Escherichia coli, the CcmG protein always acts as a weak reductant in the electron transport chain during cytochrome c maturation (Ccm). Here we report (1)H, (15)N and (13)C backbone and side-chain resonance assignments of the reduced CcmG protein (residues 19-185, renumbered as 1-167) from E. coli. This work lays the essential basis for the further structural and functional analysis of reduced CcmG.
authors.affiliation: The Key Laboratory for Chemical Biology of Fujian Province, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China.
authors.forename: Chengyan
authors.initials: C
authors.lastname: Wu
authors.forename: Jing
authors.initials: J
authors.lastname: Hong
authors.forename: Xinli
authors.initials: X
authors.lastname: Liao
authors.forename: Chenyun
authors.initials: C
authors.lastname: Guo
authors.forename: Xueji
authors.initials: X
authors.lastname: Wu
authors.forename: Hongyu
authors.initials: H
authors.lastname: Hu
authors.forename: Donghai
authors.initials: D
authors.lastname: Lin
mesh_terms: D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011490:Protein Disulfide Reductase (Glutathione) / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; C485980:Ccmg protein, E coli; D011490:Protein Disulfide Reductase (Glutathione)