Summary for 2GLT
| Entry DOI | 10.2210/pdb2glt/pdb |
| Descriptor | GLUTATHIONE BIOSYNTHETIC LIGASE (2 entities in total) |
| Functional Keywords | glutathione biosynthesis ligase, biosynthesis, ligase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 35601.82 |
| Authors | Matsuda, K.,Yamaguchi, H.,Kato, H.,Nishioka, T.,Katsube, Y.,Oda, J. (deposition date: 1995-05-16, release date: 1995-07-31, Last modification date: 2024-05-29) |
| Primary citation | Matsuda, K.,Mizuguchi, K.,Nishioka, T.,Kato, H.,Go, N.,Oda, J. Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Eng., 9:1083-1092, 1996 Cited by PubMed Abstract: The crystal structure of Escherichia coli B glutathione synthetase (GSHase) has been determined at the optimal catalytic condition pH 7.5. The most significant structural difference from the structure at pH 6.0 is the movement of the central domain towards the N-terminal domain almost as a rigid body. As a result of this movement, new interdomain and intersubunit polar interactions are formed which stabilize the dimeric structure further. The structure of GSHase at optimal pH was compared with 294 other known protein structures in terms of the spatial arrangements of secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA carboxylase) were found to have structures similar to the ATP-binding site of GSHase, which extends across two domains. The ATP-binding sites in these four enzymes are composed of two antiparallel beta-sheets and are different from the classic mononucleotide-binding fold. Except for these proteins, no significant structural similarity was detected between GSHase and the other ATP-binding proteins. A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules. PubMed: 9010922DOI: 10.1093/protein/9.12.1083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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