Open AccessStructure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability
Author(s) -
Bhuiya Mohammad Wadud,
Suryadi Jimmy,
Zhou Zholi,
Brown Bernard Andrew
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113021799
Subject(s) - thermostability , pyrococcus furiosus , crystallography , archaea , biology , chemistry , biochemistry , enzyme , gene
Archaeal ribosomal protein L7Ae is a multifunctional RNA‐binding protein that directs post‐transcriptional modification of archaeal RNAs. The L7Ae protein from Aeropyrum pernix (Ap L7Ae), a member of the Crenarchaea, was found to have an extremely high melting temperature (>383 K). The crystal structure of Ap L7Ae has been determined to a resolution of 1.56 Å. The structure of Ap L7Ae was compared with the structures of two homologs: hyperthermophilic Methanocaldococcus jannaschii L7Ae and the mesophilic counterpart mammalian 15.5 kD protein. The primary stabilizing feature in the Ap L7Ae protein appears to be the large number of ion pairs and extensive ion‐pair network that connects secondary‐structural elements. To our knowledge, Ap L7Ae is among the most thermostable single‐domain monomeric proteins presently observed.