The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture

Authors

  • Ae Kyung Park,

    1. Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea
    Search for more papers by this author
  • Jin Ho Moon,

    1. Institute of Life Sciences and Natural Resources, Korea University, Seoul 136-713, Republic of Korea
    Search for more papers by this author
  • Eun Hyuk Jang,

    1. Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea
    Search for more papers by this author
  • Hyun Park,

    1. Korea Polar Research Institute, Korea Ocean Research and Development Institute, Songdo-Dong 7-50, Yeonsu-Gu, Incheon 406-840, Republic of Korea
    Search for more papers by this author
  • In Young Ahn,

    1. Korea Polar Research Institute, Korea Ocean Research and Development Institute, Songdo-Dong 7-50, Yeonsu-Gu, Incheon 406-840, Republic of Korea
    Search for more papers by this author
  • Ki Seog Lee,

    Corresponding author
    1. Department of Clinical Laboratory Science, College of Health Sciences, Catholic University of Pusan, Busan 609-757, Republic of Korea
    • Department of Clinical Laboratory, Science, College of Health Sciences, Catholic University of Pusan, Busan, 609-757, Republic of Korea
    Search for more papers by this author
  • Young Min Chi

    Corresponding author
    1. Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea
    • Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea
    Search for more papers by this author

Abstract

Glutathione-S-transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST, but there are several unique features of LeGST that may justify reclassification, which could represent specific shellfish GSTs. Here, we determined the crystal structure of LeGST, which is a shellfish specific class of GST. The structural analysis showed that the relatively open and wide hydrophobic H-site of the LeGST allows this GST to accommodate various substrates. These results suggest that the H-site of LeGST may be the result of adaptation to their environments as sedentary organisms. Proteins 2013. © 2012 Wiley Periodicals, Inc.

Ancillary