Associate Professor, Biological Chemistry
B.S., University of Science & Technology of China
Ph.D., University of Minnesota.
Postdoctoral, Yale University
The goal of our laboratory is to understand the molecular mechanisms by which the cell mediates protein folding and secretion. Despite decades of effort, the protein-folding problem remains one of the most challenging questions in molecular biology. In addition, protein folding inside the cell often faces difficulty, leading to misfolding and aggregation. To overcome these problems, cells have developed sophisticated mechanisms ranging from simple chaperoning, to active folding assistance, to the complex unfolded protein response (UPR). Protein folding problems have been directly linked to many disease states including cystic fibrosis, diabetes, various clotting disorders, and neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. We use protein crystallography to study the structures of proteins directly related to in vivo protein folding, secretion and the stress response.
1992 Bacaner Research Award
1999 Biological Scholar, University of Michigan Medical School
2001 Pew Scholars Program in Biomedical Sciences
2003 Basic Science Research Award (Deanâ€™s award)
Zhu, M., Shao, F., Innes, R. W., Dixon, J. E., and Xu, Z. (2003) The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc. Natl. Acad. Sci. USA . PMID: 14694194
Zhou, J., and Xu, Z. (2003) Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nature Struct. Biol. . PMID: 14517549
Peisach, D., Gee, P., Kent, K. and Xu, Z. (2003) The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. Structure , 11 , 703-713. PMID: 12791258
Liu, C. Y., Xu, Z. , and Kaufman, R. J. (2003) Structure and intermolecular interactions of the luminal dimerization domain of human IRE1a. J. Biol. Chem ., 278 , 17680-17687. PMID: 12637535
Xu, Z ., Knafels, J. D. Yoshino, K. (2000) The crystal structure of SecB, a bacterial chaperone dedicated for protein translocation. Nature Struct. Biol, 7 , 1172 - 1177. PMID: 11101901
Orth, K., Xu. Z ., Mudgett, M. B., Bao, Z. Q., Palmer, L., Bliska, J. B., Mangel, W. F., Staskawicz, B., Dixon, J. E. (2000) Yersinia effector YopJ is a ubiquitin-like protein protease that disrupts signaling. Scienc e, 290 , 1594 - 1597. PMID: 11090361