13C, 15N and 1H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6
Tóm tắt
Từ khóa
Tài liệu tham khảo
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
Foit L, George JS, Zhang BW, Brooks CL 3rd, Bardwell JC (2013) Chaperone activation by unfolding. Proc Natl Acad Sci USA 110:E1254–E1262. doi: 10.1073/pnas.1222458110
Gajiwala KS, Burley SK (2000) HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. J Mol Biol 295:605–612. doi: 10.1006/jmbi.1999.3347
Hong W, Jiao W, Hu J, Zhang J, Liu C, Fu X, Shen D, Xia B, Chang Z (2005) Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem 280:27029–27034. doi: 10.1074/jbc.M503934200
Hong W, Wu YE, Fu X, Chang Z (2012) Chaperone-dependent mechanisms for acid resistance in enteric bacteria. Trends Microbiol 20:328–335. doi: 10.1016/j.tim.2012.03.001
Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352. doi: 10.1385/1-59259-809-9:313
Koebnik R, Locher KP, Van Gelder P (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37:239–253
Malki A, Le HT, Milles S, Kern R, Caldas T, Abdallah J, Richarme G (2008) Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. J Biol Chem 283:13679–13687. doi: 10.1074/jbc.M800869200
Tapley TL, Korner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC (2009) Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci USA 106:5557–5562. doi: 10.1073/pnas.0811811106