2ZJ4
Isomerase domain of human glucose:fructose-6-phosphate amidotransferase
Summary for 2ZJ4
| Entry DOI | 10.2210/pdb2zj4/pdb |
| Related | 2ZJ3 |
| Descriptor | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1, 2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE (3 entities in total) |
| Functional Keywords | glucosamine-6-phosphate synthase, aldose/ketose isomerase, rossmann-like fold, transferase, alternative splicing, aminotransferase, glutamine amidotransferase, phosphoprotein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 42580.30 |
| Authors | Nakaishi, Y.,Bando, M.,Kondo, K.,Tsuge, H. (deposition date: 2008-02-29, release date: 2009-01-13, Last modification date: 2023-11-01) |
| Primary citation | Nakaishi, Y.,Bando, M.,Shimizu, H.,Watanabe, K.,Goto, F.,Tsuge, H.,Kondo, K.,Komatsu, M. Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes Febs Lett., 583:163-167, 2009 Cited by PubMed Abstract: Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes. PubMed: 19059404DOI: 10.1016/j.febslet.2008.11.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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