The rhomboid protease GlpG has weak interaction energies in its active site hydrogen bond network

Intramembrane rhomboid proteases are of particular interest because of their function to hydrolyze a peptide bond of a substrate buried in the membrane. Crystal structures of the bacterial rhomboid protease GlpG have revealed a catalytic dyad (Ser201-His254) and oxyanion hole (His150/Asn154/the back...

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Detalles Bibliográficos
Autores principales: Gaffney, Kristen A., Hong, Heedeok
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2019
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6400518/
https://www.ncbi.nlm.nih.gov/pubmed/30420443
http://dx.doi.org/10.1085/jgp.201812047

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6400518/
https://www.ncbi.nlm.nih.gov/pubmed/30420443
http://dx.doi.org/10.1085/jgp.201812047

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