8IYI

Spermidine synthase from Kluyveromyces lactis

8IYI の概要

• エントリーDOI: 10.2210/pdb8iyi/pdb
• 分子名称: KLLA0B09372p (2 entities in total)
• 機能のキーワード: spermidine, synthase, aminopropyltransferase, transferase
• 由来する生物種: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast, Candida sphaerica)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66585.56

構造登録者

Kim, S.,Chang, J.H. (登録日: 2023-04-05, 公開日: 2023-06-28, 最終更新日: 2024-05-29)

主引用文献

Kim, S.,Chang, J.H.
Structural Analysis of Spermidine Synthase from Kluyveromyces lactis.
Molecules, 28:-, 2023

PubMed Abstract: Spermidine is a polyamine molecule that performs various cellular functions, such as DNA and RNA stabilization, autophagy modulation, and eIF5A formation, and is generated from putrescine by aminopropyltransferase spermidine synthase (SpdS). During synthesis, the aminopropyl moiety is donated from decarboxylated S-adenosylmethionine to form putrescine, with 5'-deoxy-5'-methylthioadenosine being produced as a byproduct. Although the molecular mechanism of SpdS function has been well-established, its structure-based evolutionary relationships remain to be fully understood. Moreover, only a few structural studies have been conducted on SpdS from fungal species. Here, we determined the crystal structure of an apo-form of SpdS from (SpdS) at 1.9 Å resolution. Structural comparison with its homologs revealed a conformational change in the α6 helix linked to the gate-keeping loop, with approximately 40° outward rotation. This change caused the catalytic residue Asp170 to move outward, possibly due to the absence of a ligand in the active site. These findings improve our understanding of the structural diversity of SpdS and provide a missing link that expands our knowledge of the structural features of SpdS in fungal species.

PubMed: 37110680
DOI: 10.3390/molecules28083446

実験手法

X-RAY DIFFRACTION (1.9 Å)