Solution Structure and Dynamics of the Small Protein HVO_2922 from Haloferax volcanii
| العنوان: | Solution Structure and Dynamics of the Small Protein HVO_2922 from Haloferax volcanii |
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| المؤلفون: | Hendrik R. A. Jonker, Sandra Schreiber, Krishna Saxena, Anita Marchfelder, Nina Kubatova, Harald Schwalbe, Verena Vogel, Christian Richter |
| المصدر: | ChemBioChem. 21:149-156 |
| بيانات النشر: | Wiley, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Models, Molecular, Protein Conformation, Archaeal Proteins, Dimer, ved/biology.organism_classification_rank.species, Mutagenesis (molecular biology technique), Protein aggregation, 010402 general chemistry, 01 natural sciences, Biochemistry, chemistry.chemical_compound, Model organism, Haloferax volcanii, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, biology, Protein Stability, 010405 organic chemistry, Chemistry, ved/biology, Organic Chemistry, biology.organism_classification, 0104 chemical sciences, Solutions, Proteome, Haloarchaea, Thermodynamics, Molecular Medicine, Domain of unknown function |
| الوصف: | Past sequencing campaigns overlooked small proteins as they seemed to be irrelevant due to their small size. However, their occurrence is widespread, and there is growing evidence that these small proteins are in fact functionally very important in organisms found in all kingdoms of life. Within a global proteome analysis for small proteins of the archaeal model organism Haloferax volcanii, the HVO_2922 protein has been identified. It is differentially expressed in response to changes in iron and salt concentrations, thus suggesting that its expression is stress-regulated. The protein is conserved among Haloarchaea and contains an uncharacterized domain of unknown function (DUF1508, UPF0339 family protein). We elucidated the NMR solution structure, which shows that the isolated protein forms a symmetrical dimer. The dimerization is found to be concentration-dependent and essential for protein stability and most likely for its functionality, as mutagenesis at the dimer interface leads to a decrease in stability and protein aggregation. |
| تدمد: | 1439-7633 1439-4227 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f3f8129e541a5ca920ef30792d6574fTest https://doi.org/10.1002/cbic.201900085Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....1f3f8129e541a5ca920ef30792d6574f |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14397633 14394227 |
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