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Structure of nitrilotriacetate monooxygenase component B from Mycobacterium thermoresistibile.
Title | Structure of nitrilotriacetate monooxygenase component B from Mycobacterium thermoresistibile. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Zhang, Y, Edwards, TE, Begley, DW, Abramov, A, Thompkins, KB, Ferrell, M, Guo, WJ, Phan, I, Olsen, C, Napuli, A, Sankaran, B, Stacy, R, Van Voorhis, WC, Stewart, LJ, Myler, PJ |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 67 |
Issue | Pt 9 |
Pagination | 1100-5 |
Date Published | 2011 Sep 1 |
ISSN | 1744-3091 |
Keywords | Amino Acid Sequence, Conserved Sequence, Mixed Function Oxygenases, Models, Molecular, Molecular Sequence Data, Mycobacterium, Protein Structure, Tertiary, Sequence Alignment |
Abstract | 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. |
DOI | 10.1107/S1744309111012541 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 21904057 |