3qaw

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

spinqualitylabelsall models 3qaw, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qaw is a 1 chain structure with sequence from Laternula elliptica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GSH Related: 3qav Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. (c) 2012 Wiley Periodicals, Inc. The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture.,Park AK, Moon JH, Jang EH, Park H, Ahn IY, Lee KS, Chi YM Proteins. 2013 Mar;81(3):531-7. doi: 10.1002/prot.24208. Epub 2012 Dec 24. PMID:23152139 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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