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 1H, 15N and 13C 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.
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Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRpipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Di Matteo A, Calosci N, Gianni S, Jemth P, Brunori M, Travaglini-Allocatelli C (2010) Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatus. Proteins 78:2213–2221
Edeling MA, Ahuja U, Heras B, Thöny-Meyer L, Martin JL (2004) The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli. J Bacteriol 186:4030–4033
Fabianek RA, Huber-Wunderlich M, Glockshuber R, Künzler P, Hennecke H, Thöny-Meyer L (1997) Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes. J Biol Chem 272:4467–4473
Fabianek RA, Hennecke H, Thöny-Meyer L (1998) The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo. J Bacteriol 180:1947–1950
Goddard TD, Kneller DG (1993) SPARKY 3. University of California, San Francisco
Monika EM, Goldman BS, Beckman DL, Kranz RG (1997) A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis; in vitro and in vivo studies. J Mol Biol 271:679–692
Ortenberg R, Beckwith J (2003) Functions of thiol-disulfide oxidoreductases in E. coli redox myths, realities, and practicalities. Antioxid Redox Signal 5:403–411
Ouyang N, Gao YG, Hu HY, Xia ZX (2006) Crystal structure of E. coli CcmG and its mutants reveal key roles of the N-terminal β-sheet and the fingerprint region. Proteins 65:1021–1031
Ow YP, Green DR, Hao Z, Mak TW (2008) Cytochrome c: functions beyond respiration. Nat Rev Mol Cell Biol 9:532–542
Richard-Fogal CL, Frawley ER, Bonner ER, Zhu H, San Francisco B, Kranz RG (2009) A conserved haem redox and trafficking pathway for cofactor attachment. EMBO J 28:2349–2359
Stirnimann CU, Rozhkova A, Grauschopf U, Grütter MG, Glockshuber R, Capitani G (2005) Structural basis and kinetics of DsbD-dependent cytochrome c maturation. Structure 13:985–993
Turkarslan S, Sanders C, Ekici S, Daldal F (2008) Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation. Mol Microbiol 70:652–666
Wishart DS, Sykes BD (1994) The 13C chemical shift index. A simple method for the identification of protein secondary structure using 13C chemical shift data. J Biomol NMR 4:171–180
Acknowledgments
This work was supported by grants from the Natural Science Foundation of Fujian Province (No. 2011J01246), Natural Science Foundation of China (Nos. 30900233, 31170717, 91129713), and the Program of Shanghai Subject Chief Scientist (No. 09XD1405100).
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Wu, C., Hong, J., Liao, X. et al. 1H, 13C and 15N backbone and side-chain resonance assignments of reduced CcmG from Escherichia coli . Biomol NMR Assign 7, 105–108 (2013). https://doi.org/10.1007/s12104-012-9389-7
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DOI: https://doi.org/10.1007/s12104-012-9389-7