Structural highlights
Function
A0A2I5T5Y7_SERS3
Publication Abstract from PubMed
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 alpha-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.
Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.,Pramono H, Yoshida A, Hirashima Y, Sone Y, Terada T, Kosono S, Nishiyama M FEBS Lett. 2024 Dec 1. doi: 10.1002/1873-3468.15068. PMID:39618122[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2024 Dec 1. PMID:39618122 doi:10.1002/1873-3468.15068
