Get access
Advertisement

Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc

Authors

  • Sheng-Chia Chen,

    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    2. Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan
    Search for more papers by this author
    • Sheng-Chia Chen and Chi-Hung Huang contributed equally to this work.

  • Chi-Hung Huang,

    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    2. Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan
    3. Institute of Biochemistry, National Chung-Hsing University, Taichung, Taiwan
    Search for more papers by this author
    • Sheng-Chia Chen and Chi-Hung Huang contributed equally to this work.

  • Chia Shin Yang,

    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    2. Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan
    Search for more papers by this author
  • Jai-Shin Liu,

    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    Search for more papers by this author
  • Shu-Min Kuan,

    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    Search for more papers by this author
  • Yeh Chen

    Corresponding author
    1. Department of Biotechnology, Hungkuang University, Taichung, Taiwan
    Search for more papers by this author

ABSTRACT

Uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-N-acetylmannosamine (UDP-ManNAc), which is used in the biosynthesis of cell surface polysaccharides in bacteria. Biochemical experiments have demonstrated that mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall. Here, we present the crystal structures of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in open and closed conformations. A comparison of these crystal structures shows that upon UDP and UDP-GlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain. We also present the crystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in the closed conformation in the presence of UDP and UDP-GlcNAc. Although a structural overlay of these two closed-form structures reveals that the substrate-binding site is evolutionarily conserved, some areas of the allosteric site are distinct between the archaeal and bacterial UDP-GlcNAc 2-epimerases. This is the first report on the crystal structure of archaeal UDP-GlcNAc 2-epimerase, and our results clearly demonstrate the changes between the open and closed conformations of this enzyme. Proteins 2014; 82:1519–1526. © 2014 Wiley Periodicals, Inc.

Get access to the full text of this article

Ancillary