6LK7
crystal structure of Os1348 from Pseudomonas sp. Os17
Summary for 6LK7
Entry DOI | 10.2210/pdb6lk7/pdb |
Descriptor | Nitrile hydratase, alpha chain (2 entities in total) |
Functional Keywords | antibiotic-related protein, unknown function |
Biological source | Pseudomonas sp. Os17 |
Total number of polymer chains | 4 |
Total formula weight | 35724.35 |
Authors | Takeuchi, K.,Tsuchiya, W.,Fujimoto, Z.,Yamada, K.,Someya, N.,Yamazaki, T. (deposition date: 2019-12-18, release date: 2020-11-11, Last modification date: 2024-04-03) |
Primary citation | Takeuchi, K.,Tsuchiya, W.,Fujimoto, Z.,Yamada, K.,Someya, N.,Yamazaki, T. Discovery of an Antibiotic-Related Small Protein of Biocontrol Strain Pseudomonas sp. Os17 by a Genome-Mining Strategy. Front Microbiol, 11:605705-605705, 2020 Cited by PubMed Abstract: Many root-colonizing spp. exhibiting biocontrol activities produce a wide range of secondary metabolites that exert antibiotic effects against other microbes, nematodes, and insects in the rhizosphere. The expression of these secondary metabolites depends on the Gac/Rsm signal transduction pathway. Based on the findings of a previous genomic study on newly isolated biocontrol pseudomonad strains, we herein investigated the novel gene cluster OS3, which consists of four genes () that are located upstream of putative efflux transporter genes (). was predicted to encode an 85-aa small precursor protein, the expression of which was under the control of GacA, and an X-ray structural analysis suggested that the Os1348 protein formed a dimer. The mutational loss of the gene decreased the antibiotic activity of sp. Os17 without changing its growth rate. The genes were predicted to be involved in post-translational modifications. Intracellular levels of the protein in the deficient mutant of each gene differed from that in wild-type cells. These results suggest that Os1348 is involved in antibiotic activity and that the structure or expression of this protein is under the control of downstream gene products. PubMed: 33324389DOI: 10.3389/fmicb.2020.605705 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.903 Å) |
Structure validation
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