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5OJX

Crystal structure of regulator protein 2 (PamR2) from the pamamycin biosynthetic gene cluster of Streptomyces alboniger

Summary for 5OJX
Entry DOI10.2210/pdb5ojx/pdb
DescriptorTetR family transcription regulator (2 entities in total)
Functional Keywordstranscription regulator, tetr family transcription regulator, streptomyces alboniger, regulator protein 2, pamamycin biosynthesis, transcription
Biological sourceStreptomyces alboniger
Total number of polymer chains1
Total formula weight28250.69
Authors
Schmelz, S.,Rebets, Y.,Luzhetskyy, A.,Scrima, A. (deposition date: 2017-07-24, release date: 2018-04-11, Last modification date: 2024-01-17)
Primary citationRebets, Y.,Schmelz, S.,Gromyko, O.,Tistechok, S.,Petzke, L.,Scrima, A.,Luzhetskyy, A.
Design, development and application of whole-cell based antibiotic-specific biosensor.
Metab. Eng., 47:263-270, 2018
Cited by
PubMed Abstract: Synthetic biology techniques hold great promise for optimising the production of natural products by microorganisms. However, evaluating the phenotype of a modified bacterium represents a major bottleneck to the engineering cycle - particularly for antibiotic-producing actinobacteria strains, which grow slowly and are challenging to genetically manipulate. Here, we report the generation and application of antibiotic-specific whole-cell biosensor derived from TetR transcriptional repressor for use in identifying and optimising antibiotic producers. The constructed biosensor was successfully used to improve production of polyketide antibiotic pamamycin. However, an initial biosensor based on native genetic elements had inadequate dynamic and operating ranges. To overcome these limitations, we fine-tuned biosensor performance through alterations of the promoter and operator of output module and the ligand affinity of transcription factor module, which enabled us to deduce recommendations for building and application of actinobacterial biosensors.
PubMed: 29609044
DOI: 10.1016/j.ymben.2018.03.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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