5BS2

Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail

5BS2 の概要

• エントリーDOI: 10.2210/pdb5bs2/pdb
• 分子名称: Ribulose bisphosphate carboxylase large chain,CrRbcX-IIa, Ribulose bisphosphate carboxylase large chain (3 entities in total)
• 機能のキーワード: rbcx, chaperone
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• 細胞内の位置: Plastid, chloroplast: P00877
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30687.97

構造登録者

Bracher, A.,Hauser, T.,Liu, C.,Hartl, F.U.,Hayer-Hartl, M. (登録日: 2015-06-01, 公開日: 2015-08-05, 最終更新日: 2024-01-10)

主引用文献

Bracher, A.,Hauser, T.,Liu, C.,Hartl, F.U.,Hayer-Hartl, M.
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.
Plos One, 10:e0135448-e0135448, 2015

PubMed Abstract: The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.

PubMed: 26305355
DOI: 10.1371/journal.pone.0135448

実験手法

X-RAY DIFFRACTION (1.97 Å)