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| Natura: | Artículo científico |
| Lingua: | en |
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Communications biology
2024
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39433970/ |
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| _version_ | 1868266290194415618 |
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| author | Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan |
| author_facet | Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan |
| collection | PubMed - marine biology |
| contents | Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus. Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan Coenzyme A Ligases Crystallography, X-Ray Phylogeny Models, Molecular Protein Conformation Amino Acid Sequence Archaeal Proteins 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. |
| format | Artículo científico |
| id | pubmed_39433970 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Communications biology |
| record_format | pubmed |
| spellingShingle | Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus. Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan Coenzyme A Ligases Crystallography, X-Ray Phylogeny Models, Molecular Protein Conformation Amino Acid Sequence Archaeal Proteins Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus. Johnson, Jerome Tolar, Bradley B Tosun, Bilge Yoshikuni, Yasuo Francis, Christopher A Wakatsuki, Soichi DeMirci, Hasan Coenzyme A Ligases Crystallography, X-Ray Phylogeny Models, Molecular Protein Conformation Amino Acid Sequence Archaeal Proteins 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. |
| title | Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus. |
| topic | Coenzyme A Ligases Crystallography, X-Ray Phylogeny Models, Molecular Protein Conformation Amino Acid Sequence Archaeal Proteins |
| url | https://pubmed.ncbi.nlm.nih.gov/39433970/ |