2JX5

Solution structure of the ubiquitin domain N-terminal to the S27a ribosomal subunit of Giardia lamblia

2JX5 の概要

• エントリーDOI: 10.2210/pdb2jx5/pdb
• NMR情報: BMRB: 15547
• 分子名称: GlUb(S27a) (1 entity in total)
• 機能のキーワード: ubiquitin, ribosome, recombination, glub, evolution, ribosomal protein
• 由来する生物種: Giardia lamblia ATCC 50803
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7304.32

構造登録者

Catic, A.,Sun, Z.J.,Ratner, D.M.,Misaghi, S.,Spooner, E.,Samuelson, J.,Wagner, G.,Ploegh, H.L. (登録日: 2007-11-07, 公開日: 2007-12-04, 最終更新日: 2024-05-29)

主引用文献

Catic, A.,Sun, Z.J.,Ratner, D.M.,Misaghi, S.,Spooner, E.,Samuelson, J.,Wagner, G.,Ploegh, H.L.
Sequence and structure evolved separately in a ribosomal ubiquitin variant
EMBO J., 26:3474-3483, 2007

PubMed Abstract: Encoded by a multigene family, ubiquitin is expressed in the form of three precursor proteins, two of which are fusions to the ribosomal subunits S27a and L40. Ubiquitin assists in ribosome biogenesis and also functions as a post-translational modifier after its release from S27a or L40. However, several species do not conserve the ribosomal ubiquitin domains. We report here the solution structure of a distant variant of ubiquitin, found at the N-terminus of S27a in Giardia lamblia, referred to as GlUb(S27a). Despite the considerable evolutionary distance that separates ubiquitin from GlUb(S27a), the structure of GlUb(S27a) is largely identical to that of ubiquitin. The variant domain remains attached to S27a and is part of the assembled holoribosome. Thus, conservation of tertiary structure suggests a role of this variant as a chaperone, while conservation of the primary structure--necessary for ubiquitin's function as a post-translational modifier--is no longer required. Based on these observations, we propose a model to explain the origin of the widespread ubiquitin superfold in eukaryotes.

PubMed: 17599068
DOI: 10.1038/sj.emboj.7601772

実験手法

SOLUTION NMR