Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity

FKBP22, an Escherichia coli-specific peptidyl-prolyl cis-trans isomerase, shows substantial homology with the Mip-like virulence factors. Mip-like proteins are homodimeric and possess a V-shaped conformation. Their N-terminal domains form dimers, whereas their C-terminal domains bind protein/peptide...

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Detalles Bibliográficos
Autores principales: Polley, Soumitra, Chakravarty, Devlina, Chakrabarti, Gopal, Chattopadhyaya, Rajagopal, Sau, Subrata
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2015
Materias:
Research paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5889476/
https://www.ncbi.nlm.nih.gov/pubmed/29632827
http://dx.doi.org/10.1016/j.biopen.2015.07.001

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5889476/
https://www.ncbi.nlm.nih.gov/pubmed/29632827
http://dx.doi.org/10.1016/j.biopen.2015.07.001

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