Summary for 8WZU
| Entry DOI | 10.2210/pdb8wzu/pdb |
| Descriptor | 4-hydroxybutyrate--CoA ligase [ADP-forming], SULFATE ION (3 entities in total) |
| Functional Keywords | nitropumilus maritimus, acd, synthetase, hb/hp, carbon fixation, thaumarchaeota, ligase |
| Biological source | Nitrosopumilus maritimus SCM1 |
| Total number of polymer chains | 2 |
| Total formula weight | 151647.84 |
| Authors | Johnson, J.,Demirci, H. (deposition date: 2023-11-02, release date: 2024-06-12, Last modification date: 2025-06-25) |
| Primary citation | 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 Cited by 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: 39433970DOI: 10.1038/s42003-024-06432-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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