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Crystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional proteinCrystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional protein
Structural highlights
FunctionRL7A_AERPE Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedArchaeal 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 A. 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. Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.,Bhuiya MW, Suryadi J, Zhou Z, Brown BA 2nd Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):979-88. doi: , 10.1107/S1744309113021799. Epub 2013 Aug 19. PMID:23989144[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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