Structure of nitrilotriacetate monooxygenase component B fromMycobacterium thermoresistibile
| العنوان: | Structure of nitrilotriacetate monooxygenase component B fromMycobacterium thermoresistibile |
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| المؤلفون: | Christian Olsen, Wenjin Guo, Thomas E. Edwards, Isabelle Phan, Ariel Abramov, Peter J. Myler, Micah Ferrell, W. C. Van Voorhis, Lance Stewart, Kaitlin Thompkins, Darren W. Begley, Banumathi Sankaran, Yang Zhang, Robin Stacy, Alberto J. Napuli |
| المصدر: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| بيانات النشر: | International Union of Crystallography (IUCr), 2011. |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | Models, Molecular, Stereochemistry, Mycobacterium thermoresistible, Molecular Sequence Data, Biophysics, Flavin mononucleotide, Flavin group, Protomer, SSGCID, Biochemistry, Cofactor, Mixed Function Oxygenases, Mycobacterium, chemistry.chemical_compound, Structural Biology, Genetics, Structural Communications, Amino Acid Sequence, Conserved Sequence, biology, Active site, Condensed Matter Physics, biology.organism_classification, Mycobacterium thermoresistibile, oxidoreductases, Protein Structure, Tertiary, chemistry, biology.protein, Nitrilotriacetate monooxygenase, Energy source, flavin reductases, Sequence Alignment, nitrilotriacetate monooxygenase component B |
| الوصف: | The 1.6 Å resolution crystal structure of nitrilotriacetate monooxygenase component B (NTA-MoB) from M. thermoresistibile is presented, revealing a highly conserved C-terminal tail that may modulate the activity of NTA-MoB in mycobacteria. Mycobacterium tuberculosis belongs to a large family of soil bacteria which can degrade a remarkably broad range of organic compounds and utilize them as carbon, nitrogen and energy sources. It has been proposed that a variety of mycobacteria can subsist on alternative carbon sources during latency within an infected human host, with the help of enzymes such as nitrilotriacetate monooxygenase (NTA-Mo). NTA-Mo is a member of a class of enzymes which consist of two components: A and B. While component A has monooxygenase activity and is responsible for the oxidation of the substrate, component B consumes cofactor to generate reduced flavin mononucleotide, which is required for component A activity. NTA-MoB from M. thermoresistibile, a rare but infectious close relative of M. tuberculosis which can thrive at elevated temperatures, has been expressed, purified and crystallized. The 1.6 Å resolution crystal structure of component B of NTA-Mo presented here is one of the first crystal structures determined from the organism M. thermoresistibile. The NTA-MoB crystal structure reveals a homodimer with the characteristic split-barrel motif typical of flavin reductases. Surprisingly, NTA-MoB from M. thermoresistibile contains a C-terminal tail that is highly conserved among mycobacterial orthologs and resides in the active site of the other protomer. Based on the structure, the C-terminal tail may modulate NTA-MoB activity in mycobacteria by blocking the binding of flavins and NADH. |
| تدمد: | 1744-3091 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::542cc0789b61333cb1cf38759d4ce0a8 https://doi.org/10.1107/s1744309111012541 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....542cc0789b61333cb1cf38759d4ce0a8 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17443091 |
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