3NFW

Crystal structure of nitrilotriacetate monooxygenase component B (A0R521 homolog) from Mycobacterium thermoresistibile

Summary for 3NFW

• Entry DOI: 10.2210/pdb3nfw/pdb
• Descriptor: Flavin reductase-like, FMN-binding protein, GLYCEROL (3 entities in total)
• Functional Keywords: seattle structural genomics center for infectious disease, ssgcid, mycobacterium, tuberculosis, thermoresistible, biodegredation, nadh dependent, oxidoreductase
• Biological source: Mycobacterium thermoresistibile
• Total number of polymer chains: 4
• Total formula weight: 93321.18

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-06-10, release date: 2010-06-23, Last modification date: 2023-09-06)

Primary citation

Zhang, Y.,Edwards, T.E.,Begley, D.W.,Abramov, A.,Thompkins, K.B.,Ferrell, M.,Guo, W.J.,Phan, I.,Olsen, C.,Napuli, A.,Sankaran, B.,Stacy, R.,Van Voorhis, W.C.,Stewart, L.J.,Myler, P.J.
Structure of nitrilotriacetate monooxygenase component B from Mycobacterium thermoresistibile.
Acta Crystallogr.,Sect.F, 67:1100-1105, 2011

PubMed 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.

PubMed: 21904057
DOI: 10.1107/S1744309111012541

Experimental method

X-RAY DIFFRACTION (1.6 Å)