Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
| Autor: | Ebru Destan, Yasuo Yoshikuni, Samuel Deutsch, Esra Ayan, Bradley B. Tolar, Christopher A. Francis, Hasan DeMirci, Busra Yuksel, Soichi Wakatsuki |
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| Přispěvatelé: | Destan, Ebru, Yüksel, Büşra, Ayan, Esra, Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Tolar, Bradley B., Deutsch, Sam, Yoshikuni, Yasuo, Wakatsuki, Soichi, Francis, Christopher A., College of Sciences, Graduate School of Sciences and Engineering, Department of Molecular Biology and Genetics |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Thaumarchaeota Protein Conformation Science Archaeal Proteins Nitrosopumilus Crystallography X-Ray Nitrification Archaeon Bacteria Article Catalysis Substrate Specificity chemistry.chemical_compound Structure-Activity Relationship Biosynthesis Models Phosphofructokinase 2 Bifunctional Enoyl-CoA Hydratase chemistry.chemical_classification Crystallography Multidisciplinary biology Crotonyl-CoA Molecular Carbon Dioxide biology.organism_classification Archaea Enzyme Biochemistry chemistry Dehydratase Ammonia-oxidizing archaea Nitrifying archaea Crystal-Structure Diversity Reveals Physiology Mechanism Reductase Coenzyme X-Ray Medicine Acyl Coenzyme A Structural biology Biotechnology |
| Zdroj: | Scientific Reports Scientific reports, vol 11, iss 1 Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) |
| ISSN: | 2045-2322 |
| Popis: | The ammonia-oxidizing thaumarchaeal 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle is one of the most energy-efficient CO2 fixation cycles discovered thus far. The protein encoded by Nmar_1308 (from Nitrosopumilus maritimus SCM1) is a promiscuous enzyme that catalyzes two essential reactions within the thaumarchaeal 3HP/4HB cycle, functioning as both a crotonyl-CoA hydratase (CCAH) and 3-hydroxypropionyl-CoA dehydratase (3HPD). In performing both hydratase and dehydratase activities, Nmar_1308 reduces the total number of enzymes necessary for CO2 fixation in Thaumarchaeota, reducing the overall cost for biosynthesis. Here, we present the first high-resolution crystal structure of this bifunctional enzyme with key catalytic residues in the thaumarchaeal 3HP/4HB pathway. National Science Foundation (NSF) Science and Technology Centers; Science and Technology Centers; Scientifc and Technological Research Council of Turkey (TÜBİTAK); US Department of Energy Joint Genome Institute |
| Databáze: | OpenAIRE |
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