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6XTU

FULL-LENGTH LTTR LYSG FROM CORYNEBACTERIUM GLUTAMICUM

Summary for 6XTU
Entry DOI10.2210/pdb6xtu/pdb
DescriptorLysine export transcriptional regulatory protein LysG (2 entities in total)
Functional Keywordslttr helix-turn-helix transcription regulation, transcription
Biological sourceCorynebacterium glutamicum MB001
Total number of polymer chains2
Total formula weight67188.90
Authors
Hofmann, E.,Syberg, F.,Schlicker, C.,Eggeling, L.,Schendzielorz, G. (deposition date: 2020-01-16, release date: 2020-10-07, Last modification date: 2024-01-24)
Primary citationDella Corte, D.,van Beek, H.L.,Syberg, F.,Schallmey, M.,Tobola, F.,Cormann, K.U.,Schlicker, C.,Baumann, P.T.,Krumbach, K.,Sokolowsky, S.,Morris, C.J.,Grunberger, A.,Hofmann, E.,Schroder, G.F.,Marienhagen, J.
Engineering and application of a biosensor with focused ligand specificity.
Nat Commun, 11:4851-4851, 2020
Cited by
PubMed Abstract: Cell factories converting bio-based precursors to chemicals present an attractive avenue to a sustainable economy, yet screening of genetically diverse strain libraries to identify the best-performing whole-cell biocatalysts is a low-throughput endeavor. For this reason, transcriptional biosensors attract attention as they allow the screening of vast libraries when used in combination with fluorescence-activated cell sorting (FACS). However, broad ligand specificity of transcriptional regulators (TRs) often prohibits the development of such ultra-high-throughput screens. Here, we solve the structure of the TR LysG of Corynebacterium glutamicum, which detects all three basic amino acids. Based on this information, we follow a semi-rational engineering approach using a FACS-based screening/counterscreening strategy to generate an L-lysine insensitive LysG-based biosensor. This biosensor can be used to isolate L-histidine-producing strains by FACS, showing that TR engineering towards a more focused ligand spectrum can expand the scope of application of such metabolite sensors.
PubMed: 32978386
DOI: 10.1038/s41467-020-18400-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.52 Å)
Structure validation

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