The structure of a shellfish specific GST class glutathione S‐transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture |
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| Authors: | Ae Kyung Park Jin Ho Moon Eun Hyuk Jang Hyun Park In Young Ahn Ki Seog Lee Young Min Chi |
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| Affiliation: | 1. Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136‐713, Republic of Korea;2. Institute of Life Sciences and Natural Resources, Korea University, Seoul 136‐713, Republic of Korea;3. Korea Polar Research Institute, Korea Ocean Research and Development Institute, Songdo‐Dong 7‐50, Yeonsu‐Gu, Incheon 406‐840, Republic of Korea;4. Department of Clinical Laboratory Science, College of Health Sciences, Catholic University of Pusan, Busan 609‐757, Republic of Korea |
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| 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. |
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| Keywords: | glutathione‐S‐transferases marine organisms Antarctic bivalve Laternula elliptica shellfish specific GST |
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