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2FC3

Crystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional protein

Summary for 2FC3
Entry DOI10.2210/pdb2fc3/pdb
Descriptor50S ribosomal protein L7Ae (2 entities in total)
Functional Keywordsalpha-beta-alpha sandwich, ribosome, rna binding protein
Biological sourceAeropyrum pernix
Cellular locationCytoplasm : Q9YAX7
Total number of polymer chains1
Total formula weight13627.87
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 citationBhuiya, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

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