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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...
| Autores principales: | , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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Rockefeller University Press
2019
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| 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 |