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Filters: Author is Su, Chih-Chia  [Clear All Filters]
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Su, C. - C., Bolla, J. Reddy, Kumar, N., Radhakrishnan, A., Long, F., Delmar, J. A., Chou, T. - H., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2015) Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps. Cell Rep. 11, 61-70
Su, C. - C., Radhakrishnan, A., Kumar, N., Long, F., Bolla, J. Reddy, Lei, H. - T., Delmar, J. A., Do, S. V., Chou, T. - H., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2014) Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. Protein Sci. 23, 954-61
Su, C. - C., Yin, L., Kumar, N., Dai, L., Radhakrishnan, A., Bolla, J. Reddy, Lei, H. - T., Chou, T. - H., Delmar, J. A., Rajashankar, K. R., Zhang, Q., Shin, Y. - K., and Yu, E. W. (2017) Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. Nat Commun. 8, 171
Su, C. - C., Long, F., Lei, H. - T., Bolla, J. Reddy, Do, S. V., Rajashankar, K. R., and Yu, E. W. (2012) Charged amino acids (R83, E567, D617, E625, R669, and K678) of CusA are required for metal ion transport in the Cus efflux system. J Mol Biol. 422, 429-41
Su, C. - C., Long, F., Zimmermann, M. T., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2011) Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature. 470, 558-62
Su, C. - C., Long, F., and Yu, E. W. (2011) The Cus efflux system removes toxic ions via a methionine shuttle. Protein Sci. 20, 6-18
Su, C. - C., Yang, F., Long, F., Reyon, D., Routh, M. D., Kuo, D. W., Mokhtari, A. K., Van Ornam, J. D., Rabe, K. L., Hoy, J. A., Lee, Y. Jin, Rajashankar, K. R., and Yu, E. W. (2009) Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol. 393, 342-55
Su, C. - C., Long, F., McDermott, G., Shafer, W. M., and Yu, E. W. (2008) Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64, 289-92
Su, C. - C., Klenotic, P. A., Bolla, J. Reddy, Purdy, G. E., Robinson, C. V., and Yu, E. W. (2019) MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine. Proc Natl Acad Sci U S A. 10.1073/pnas.1901346116
Su, C. - C., Klenotic, P. A., Cui, M., Lyu, M., Morgan, C. E., and Yu, E. W. (2021) Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol. 19, e3001370