Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of l-tryptophan

The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand l-tryptophan (l-Trp) indicate that l-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts....

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Detalles Bibliográficos
Autores principales: Sprenger, Janina, Lawson, Catherine L., von Wachenfeldt, Claes, Lo Leggio, Leila, Carey, Jannette
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8248821/
https://www.ncbi.nlm.nih.gov/pubmed/34196612
http://dx.doi.org/10.1107/S2053230X21006142

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8248821/
https://www.ncbi.nlm.nih.gov/pubmed/34196612
http://dx.doi.org/10.1107/S2053230X21006142

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