8WZU

4-hydroxybutyryl-CoA Synthetase (ADP-forming) from Nitrosopumilus maritimus.

「8IUP」から置き換えられました

8WZU の概要

• エントリーDOI: 10.2210/pdb8wzu/pdb
• 分子名称: 4-hydroxybutyrate--CoA ligase [ADP-forming], SULFATE ION (3 entities in total)
• 機能のキーワード: nitropumilus maritimus, acd, synthetase, hb/hp, carbon fixation, thaumarchaeota, ligase
• 由来する生物種: Nitrosopumilus maritimus SCM1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 151647.84

構造登録者

Johnson, J.,Demirci, H. (登録日: 2023-11-02, 公開日: 2024-06-12, 最終更新日: 2025-06-25)

主引用文献

Johnson, J.,Tolar, B.B.,Tosun, B.,Yoshikuni, Y.,Francis, C.A.,Wakatsuki, S.,DeMirci, H.
Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus.
Commun Biol, 7:1364-1364, 2024

PubMed Abstract: The 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle from ammonia-oxidizing Thaumarchaeota is currently considered the most energy-efficient aerobic carbon fixation pathway. The Nitrosopumilus maritimus 4-hydroxybutyryl-CoA synthetase (ADP-forming; Nmar_0206) represents one of several enzymes from this cycle that exhibit increased efficiency over crenarchaeal counterparts. This enzyme reduces energy requirements on the cell, reflecting thaumarchaeal success in adapting to low-nutrient environments. Here we show the structure of Nmar_0206 from Nitrosopumilus maritimus SCM1, which reveals a highly conserved interdomain linker loop between the CoA-binding and ATP-grasp domains. Phylogenetic analysis suggests the widespread prevalence of this loop and highlights both its underrepresentation within the PDB and structural importance within the (ATP-forming) acyl-CoA synthetase (ACD) superfamily. This linker is shown to have a possible influence on conserved interface interactions between domains, thereby influencing homodimer stability. These results provide a structural basis for the energy efficiency of this key enzyme in the modified 3HP/4HB cycle of Thaumarchaeota.

PubMed: 39433970
DOI: 10.1038/s42003-024-06432-x

実験手法

X-RAY DIFFRACTION (2.8 Å)