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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):979-88. doi: 10.1107/S1744309113021799. Epub 2013 Aug 19.

Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.

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  • 1Conagen Inc., Saint Louis, MO 63132, USA. wadud@conagen-inc.com

Abstract

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.

KEYWORDS:

Aeropyrum pernix; L7Ae; ion pairs; ribosomal proteins; thermal stability

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