2FC3

Crystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional protein

2FC3 の概要

• エントリーDOI: 10.2210/pdb2fc3/pdb
• 分子名称: 50S ribosomal protein L7Ae (2 entities in total)
• 機能のキーワード: alpha-beta-alpha sandwich, ribosome, rna binding protein
• 由来する生物種: Aeropyrum pernix
• 細胞内の位置: Cytoplasm : Q9YAX7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13627.87

構造登録者

Brown II, B.A.,Suryadi, J.,Zhou, Z.,Gupton Jr., T.B.,Flowers, S.L. (登録日: 2005-12-11, 公開日: 2006-11-28, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.56 Å)