Cover Picture: Insights into TIM-Barrel Prenyl Transferase Mechanisms: Crystal Structures of PcrB from Bacillus subtilis and Staphylococcus aureus (ChemBioChem 2/2013)

Authors

  • Feifei Ren,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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    • These authors contributed equally to this work.

  • Xinxin Feng,

    1. Department of Chemistry, University of Illinois, 600 South Mathews Ave. Urbana, IL 61801 (USA)
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    • These authors contributed equally to this work.

  • Dr. Tzu-Ping Ko,

    1. Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 11529 (Taiwan)
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    • These authors contributed equally to this work.

  • Dr. Chun-Hsiang Huang,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Yumei Hu,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Dr. Hsiu-Chien Chan,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Yi-Liang Liu,

    1. Department of Chemistry, University of Illinois, 600 South Mathews Ave. Urbana, IL 61801 (USA)
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  • Dr. Ke Wang,

    1. Department of Chemistry, University of Illinois, 600 South Mathews Ave. Urbana, IL 61801 (USA)
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  • Dr. Chun-Chi Chen,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Xuefei Pang,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Miao He,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Yujie Li,

    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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  • Prof. Dr. Eric Oldfield,

    Corresponding author
    1. Department of Chemistry, University of Illinois, 600 South Mathews Ave. Urbana, IL 61801 (USA)
    • Department of Chemistry, University of Illinois, 600 South Mathews Ave. Urbana, IL 61801 (USA)
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  • Prof. Dr. Rey-Ting Guo

    Corresponding author
    1. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
    • Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 XiQiDao, Tianjin 300308 (China)
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Abstract

original image

The cover picture shows the structure of the prenyl transferase PcrB. Prenyl transferases (PTs) play a key role in isoprenoid biosynthesis, and recently a new group of PTs with a triose phosphate isomerase (TIM)-barrel fold have been discovered. The structures of PcrB from Bacillus subtilis and Staphylococcus aureus are reported here and show that there are two tyrosines and one glutamic acid in the active-site region that are poised to activate the substrate's C3 OH group for nucleophilic attack, as well as remove H+ from the active-site region. The position of the prenyl diphosphate, which binds to an essential aspartic acid via Mg2+, was also located, and by using bioinformatics and site-directed mutagenesis, a role for another tyrosine residue, in chain elongation, was demonstrated. In the article on p. 195 ff., E. Oldfield, R.-T. Guo et al. show how the results also provide a structural basis for the binding of a highly bent isoprenoid side chain in another TIM barrel PT, MoeO5.

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