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Park, E. and MacKinnon, R. (2018). Structure of the CLC-1 chloride channel from Homo sapiens. Elife. doi: 10.7554/eLife.36629

 
CLC-1.PNG
 

Active site of the human CLC-1 chloride ion channel visualized by cryo-electron microscopy (Park and MacKinnon, 2018)

Rapoport, T.A., Li, L., and Park, E. (2017). Structural and mechanistic insights into protein translocation. Annual review of cell and developmental biology. 33:369-390 (review)

Park, E., Campbell E., and MacKinnon R. (2017). Structure of a CLC-K chloride channel by cryo-electron microscopy. Nature. 541:500-505.

 
CLC-K channel.png
 

Cryo-EM Structure of a Fab-bound bovine CLC-K chloride channel (Park et al., 2017)

 

*Li, L., *Park, E., Ling, J., Ingram, J., Ploegh, H., and Rapoport, T.A. (2016). Crystal structure of a substrate-engaged SecY protein-translocation channel. Nature. 531:395-399

 
 Crystal structure of a substrate-engaged SecY protein-translocation channel enabled by a SecA-substrate fusion approach (Li and Park et al., 2016)

Crystal structure of a substrate-engaged SecY protein-translocation channel enabled by a SecA-substrate fusion approach (Li and Park et al., 2016)

 

Park, E., Ménétret, J.F., Gumbart, J.C., Ludtke, S.J., Li, W., Whynot, A., Rapoport, T.A., and Akey, C.W. (2014). Structure of the SecY channel during initiation of protein translocation. Nature. 506:102-106.

*Park, E., *Lee, J.W., *Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., and Chung, C.H. (2013). Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation. Journal of molecular biology. 425:2940-2954.

Park, E., and Rapoport, T.A. (2012). Bacterial protein translocation requires only one copy of the SecY complex in vivo. Journal of cell biology. 198:881-893.

Park, E., and Rapoport, T.A. (2012). Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annual review of biophysics. 41:21-40. (review)

Park, E., and Rapoport, T.A. (2011). Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature. 473:239-242.

 
 Mechanism by which the pore-ring residues and plug of the SecY protein-conducting channel preserve the membrane permeability barrier against ions and small molecules (Park and Rapoport, 2011)

Mechanism by which the pore-ring residues and plug of the SecY protein-conducting channel preserve the membrane permeability barrier against ions and small molecules (Park and Rapoport, 2011)

 

*Lee, J.W., *Park, E., Jeong, M.S., Jeon, Y.J., Eom, S.H., Seol, J.H., and Chung, C.H. (2009). HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis. The Journal of biological chemistry. 284:33475-33484.

*Park, E., *Lee, J.W., Eom, S.H., Seol, J.H., and Chung, C.H. (2008). Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent. The Journal of biological chemistry. 283:33258-33266.

Ménétret, J.F., Hegde, R.S., Aguiar, M., Gygi, S.P., Park, E., Rapoport, T.A., and Akey, C.W. (2008). Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome. Structure. 16:1126-1137.

Ménétret, J.F., Schaletzky, J., Clemons, W.M., Jr., Osborne, A.R., Skånland, S.S., Denison, C., Gygi, S.P., Kirkpatrick, D.S., Park, E., Ludtke, S.J., Rapoport, T.A., and Akey, C.W. (2007). Ribosome binding of a single copy of the SecY complex: implications for protein translocation. Molecular cell. 28.1083-1092.

*Lee, J.W., *Park, E., Bang, O., Eom, S.H., Cheong, G.W., Chung, C.H., and Seol, J.H. (2007). Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase. Molecules and cells. 23:252-257.

Park, E., Rho, Y.M., Koh, O.J., Ahn, S.W., Seong, I.S., Song, J.J., Bang, O., Seol, J.H., Wang, J., Eom, S.H., and Chung, C.H. (2005). Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. The Journal of biological chemistry. 280:22892-22898.

           * denotes equal contribution