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The structure of a shellfish specific GST class glutathione S-transferase from Antarctic bivalve Laternulaellipticareveals novel active site architecture.
MedLine Citation:
PMID:  23152139     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 Laternulaelliptica (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 2012. © 2012 Wiley Periodicals, Inc.
Authors:
Ae Kyung Park; Jin Ho Moon; Eunhyuk Jang; Hyun Park; In Young Ahn; Ki Seog Lee; Young Min Chi
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-14
Journal Detail:
Title:  Proteins     Volume:  -     ISSN:  1097-0134     ISO Abbreviation:  Proteins     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 Wiley Periodicals, Inc.
Affiliation:
Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, Republic of Korea.
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