2FC3

Crystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional protein

Summary for 2FC3

• Entry DOI: 10.2210/pdb2fc3/pdb
• Descriptor: 50S ribosomal protein L7Ae (2 entities in total)
• Functional Keywords: alpha-beta-alpha sandwich, ribosome, rna binding protein
• Biological source: Aeropyrum pernix
• Cellular location: Cytoplasm : Q9YAX7
• Total number of polymer chains: 1
• Total formula weight: 13627.87

Authors

Brown II, B.A.,Suryadi, J.,Zhou, Z.,Gupton Jr., T.B.,Flowers, S.L. (deposition date: 2005-12-11, release date: 2006-11-28, Last modification date: 2023-08-30)

Primary citation

Bhuiya, M.W.,Suryadi, J.,Zhou, Z.,Brown, B.A.
Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.
Acta Crystallogr.,Sect.F, 69:979-988, 2013

PubMed 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.

PubMed: 23989144
DOI: 10.1107/S1744309113021799

Experimental method

X-RAY DIFFRACTION (1.56 Å)