Professional Education

  • Doctor, Institute of Biophysics, Chinese Academy of Sciences, Biochemistry and Molecular Biology (2017)
  • Master, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Biochemistry and Molecular Biology (2012)
  • Bachelor, Beijing University of Chemical Technology, Biological Engineering (2009)

Contact

  • Academic
    hanlei@stanford.edu
    University - Scholar Department: Department of Molecular and Cellular Physiology Position: Postdoctoral Scholar

Additional Info

  • Mail Code: 5345

All Publications

  • Structure and mechanism of the alkane-oxidizing enzyme AlkB. Nature communications Guo, X., Zhang, J., Han, L., Lee, J., Williams, S. C., Forsberg, A., Xu, Y., Austin, R. N., Feng, L. 2023; 14 (1): 2180

    Abstract

    Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.

    View details for DOI 10.1038/s41467-023-37869-z

    View details for PubMedID 37069165

    View details for PubMedCentralID 4640736

  • Structure and mechanism of the SGLT family of glucose transporters. Nature Han, L., Qu, Q., Aydin, D., Panova, O., Robertson, M. J., Xu, Y., Dror, R. O., Skiniotis, G., Feng, L. 2021

    Abstract

    Glucose is a primary energy source in living cells. The discovery in 1960s that a sodium gradient powers the active uptake of glucose in the intestine1 heralded the concept of a secondary active transporter that can catalyse the movement of a substrate against an electrochemical gradient by harnessing energy from another coupled substrate. Subsequently, coupled Na+/glucose transport was found to be mediated by sodium-glucose cotransporters2,3 (SGLTs). SGLTs are responsible for active glucose and galactose absorption in the intestine and for glucose reabsorption in the kidney4, and are targeted by multiple drugs to treat diabetes5. Several members within the SGLT family transport key metabolites other than glucose2. Here we report cryo-electron microscopy structures of the prototypic human SGLT1 and a related monocarboxylate transporter SMCT1 from the same family. The structures, together with molecular dynamics simulations and functional studies, define the architecture of SGLTs, uncover the mechanism of substrate binding and selectivity, and shed light on water permeability of SGLT1. These results provide insights into the multifaceted functions of SGLTs.

    View details for DOI 10.1038/s41586-021-04211-w

    View details for PubMedID 34880492