Weikai Li, Ph.D.

Weikai Li
Assistant Professor

Biochemistry and Molecular Biophysics

Graduate Programs (DBBS)
Publications (PubMed / NIH)

Office: 251 McDonnell Science Building
Phone: 314-362-8687
Email: weikai(at)wustl.edu
 

Research

The Li lab studies intramembrane enzymes related to hematology. We have determined crystal structures of vitamin K epoxide reductase (VKOR), which is a key enzyme that supports blood coagulation and disulfide-bond formation. VKOR is the target of warfarin, the most commonly used oral anticoagulant. We have also solved the first structure in the UbiA superfamily, which synthesizes lipophilic aromatic compounds (e.g. ubiquinones) that play essential roles in biological membranes. To better understand the biological processes, we combine our structural studies with biochemistry, mass spectrometry, and cell biology approaches. The movie below shows how ubiquinones are made in membranes.

How_Quinones_Are_Made_In_Membranes1b

Publications

  • Shen G., Cui W., Zhang H., Zhou F., Huang W., Liu Q., Yang Y., Li S., Bowman G.R., Sadler J.E., Gross M.L., and Li W.
    Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer.
    Nature Structural & Molecular Biology 24, 69–76 (2017). (Abstract)
    Featured in News and Views, Nature Structural & Molecular Biology 24, 5–6 (2017).

  • Li, W. Bringing bioactive compounds into membranes: The UbiA superfamily of intramembrane aromatic prenyltransferases. Trends Biochem Sci 41:356-370 (2016). [Abstract]

  • Cheng, W. and Li, W. Structural insights into ubiquinone biosynthesis in membranes. Science 343:878-881 (2014). [Abstract]

  • Liu, S., Cheng, W., Fowle Grider, R., Shen, G. and Li, W. Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer. Nature Communications 5:3110 (2014). [Abstract]

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

  • Li, W. and Li, F. Cross-crystal averaging with search models to improve molecular replacement phases. Structure 19:155-161 (2011). [Abstract]

  • Li, W., Schulman, S., Dutton, R., Boyd, D., Beckwith, J. and Rapoport, T.A. Structure of a bacterial homolog of vitamin K epoxide reductase. Nature, 463:507-512 (2010). [Abstract]

  • Schulman, S., Wang, B., Li, W. and Rapoport, T.A. Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc Natl Acad Sci U S A 107:15027-15032 (2010). [Abstract]

  • Li, W., Schulman, S., Boyd, D., Erlandson, K., Beckwith, J. and Rapoport, T.A. The plug domain of the SecY protein stabilized the closed state of the translocation channel and maintains a membrane seal. Mol Cell 26:511-521. (2007). (Cover story.) [Abstract]

  • Li, W., Kamtekar, S., Xiong, Y, Sarkis, G.J., Grindley, N.D. and Steitz, T.A. Structure of a synaptic gamma delta resolvase tetramer covalently linked to two cleaved DNAs. Science 309:1210-1215 (2005). [Abstract]