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3QAV

Crystal structure of a glutathione S-transferase from Antarctic clam Laternula elliptica

Summary for 3QAV
Entry DOI10.2210/pdb3qav/pdb
Related3QAW
DescriptorRho-class glutathione S-transferase (2 entities in total)
Functional Keywordscytosol, transferase
Biological sourceLaternula elliptica
Total number of polymer chains1
Total formula weight27981.18
Authors
Park, A.K.,Moon, J.H.,Chi, Y.M. (deposition date: 2011-01-12, release date: 2012-02-01, Last modification date: 2024-03-20)
Primary citationPark, A.K.,Moon, J.H.,Jang, E.H.,Park, H.,Ahn, I.Y.,Lee, K.S.,Chi, Y.M.
The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture.
Proteins, 81:531-537, 2013
Cited by
PubMed 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.
PubMed: 23152139
DOI: 10.1002/prot.24208
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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数据于2025-07-23公开中

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