8Y96
Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006
Summary for 8Y96
| Entry DOI | 10.2210/pdb8y96/pdb |
| Descriptor | DegT/DnrJ/EryC1/StrS family aminotransferase, DegT/DnrJ/EryC1/StrS aminotransferase, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | aminotransferase, heterooligomer, biosynthetic protein, transferase |
| Biological source | Serratia sp. ATCC 39006 More |
| Total number of polymer chains | 4 |
| Total formula weight | 149237.00 |
| Authors | Pramono, H.,Yoshida, A.,Nishiyama, M. (deposition date: 2024-02-06, release date: 2024-12-18, Last modification date: 2025-01-22) |
| Primary citation | Pramono, H.,Yoshida, A.,Hirashima, Y.,Sone, Y.,Terada, T.,Kosono, S.,Nishiyama, M. Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function. Febs Lett., 599:74-88, 2025 Cited by PubMed Abstract: Serratia sp. ATCC 39006 has two tandemly positioned genes, ser4 and ser5, both annotated as sugar aminotransferases, in a putative secondary metabolite biosynthetic gene cluster. Ser5 possesses a complete fold-type I aminotransferase fold, while Ser4 lacks the N- and C-terminal regions and a catalytically important lysine residue of fold-type I aminotransferase. We herein revealed that Ser4 and Ser5 formed a heterotetrameric complex (SerTA) with aminotransferase activity and determined the crystal structures. MD simulations and activity assays with SerTA variants indicated that residues from helix α-8* of inactive Ser4 are important for activity, confirming the importance of heterocomplex formation for activity. Furthermore, the structures suggest that SerTA recognizes a substrate loaded on the carrier protein. PubMed: 39618122DOI: 10.1002/1873-3468.15068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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