4XOM
Coenzyme F420:L-glutamate ligase (FbiB) from Mycobacterium tuberculosis (C-terminal domain).
Summary for 4XOM
| Entry DOI | 10.2210/pdb4xom/pdb |
| Related | 4XOO 4XOQ |
| Descriptor | Coenzyme F420:L-glutamate ligase, SULFATE ION (3 entities in total) |
| Functional Keywords | nadh-oxidase fold, fmn- and f420-binding, unknown function |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 4 |
| Total formula weight | 89602.37 |
| Authors | Rehan, A.M.,Bashiri, G.,Baker, H.M.,Baker, E.N.,Squire, C.J. (deposition date: 2015-01-16, release date: 2016-02-17, Last modification date: 2024-02-28) |
| Primary citation | Bashiri, G.,Rehan, A.M.,Sreebhavan, S.,Baker, H.M.,Baker, E.N.,Squire, C.J. Elongation of the Poly-gamma-glutamate Tail of F420 Requires Both Domains of the F420: gamma-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis. J.Biol.Chem., 291:6882-6894, 2016 Cited by PubMed Abstract: Cofactor F420is an electron carrier with a major role in the oxidoreductive reactions ofMycobacterium tuberculosis, the causative agent of tuberculosis. A γ-glutamyl ligase catalyzes the final steps of the F420biosynthesis pathway by successive additions ofl-glutamate residues to F420-0, producing a poly-γ-glutamate tail. The enzyme responsible for this reaction in archaea (CofE) comprises a single domain and produces F420-2 as the major species. The homologousM. tuberculosisenzyme, FbiB, is a two-domain protein and produces F420with predominantly 5-7l-glutamate residues in the poly-γ-glutamate tail. The N-terminal domain of FbiB is homologous to CofE with an annotated γ-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Here we demonstrate that full-length FbiB adds multiplel-glutamate residues to F420-0in vitroto produce F420-5 after 24 h; communication between the two domains is critical for full γ-glutamyl ligase activity. We also present crystal structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap. Finally, we discuss the features of a full-length structural model produced by small angle x-ray scattering and its implications for the role of N- and C-terminal domains in catalysis. PubMed: 26861878DOI: 10.1074/jbc.M115.689026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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