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6LK7

crystal structure of Os1348 from Pseudomonas sp. Os17

Summary for 6LK7
Entry DOI10.2210/pdb6lk7/pdb
DescriptorNitrile hydratase, alpha chain (2 entities in total)
Functional Keywordsantibiotic-related protein, unknown function
Biological sourcePseudomonas sp. Os17
Total number of polymer chains4
Total formula weight35724.35
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 citationTakeuchi, 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: 33324389
DOI: 10.3389/fmicb.2020.605705
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.903 Å)
Structure validation

229380

數據於2024-12-25公開中

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