8Y97

Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006, PMP-bound form

8Y97 の概要

• エントリーDOI: 10.2210/pdb8y97/pdb
• 関連するPDBエントリー: 8Y96
• 分子名称: DegT/DnrJ/EryC1/StrS family aminotransferase, DegT/DnrJ/EryC1/StrS aminotransferase, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: aminotransferase, heterooligomer, biosynthetic protein, transferase
• 由来する生物種: Serratia sp. ATCC 39006; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149541.22

構造登録者

Pramono, H.,Yoshida, A.,Nishiyama, M. (登録日: 2024-02-06, 公開日: 2024-12-18, 最終更新日: 2025-01-22)

主引用文献

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

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: 39618122
DOI: 10.1002/1873-3468.15068

実験手法

X-RAY DIFFRACTION (2.83 Å)