2PY8

RbcX

2PY8 の概要

• エントリーDOI: 10.2210/pdb2py8/pdb
• 分子名称: Hypothetical protein rbcX, CHLORIDE ION, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (4 entities in total)
• 機能のキーワード: all helical fold, chaperone
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67552.52

構造登録者

Tanaka, S.,Sawaya, M.R.,Kerfeld, C.A.,Yeates, T.O. (登録日: 2007-05-15, 公開日: 2007-10-09, 最終更新日: 2024-02-21)

主引用文献

Tanaka, S.,Sawaya, M.R.,Kerfeld, C.A.,Yeates, T.O.
Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.
Acta Crystallogr.,Sect.D, 63:1109-1112, 2007

PubMed Abstract: In some cyanobacteria, the genes for the large and small subunits of the enzyme RuBisCO are separated on the bacterial chromosome by the insertion of a gene coding for a protein designated RbcX, which acts as a chaperone for RuBisCO. A recent structural study [Saschenbrecker et al. (2007), Cell, 129, 1189-1200] has shed light on the mechanism by which RbcX assists RuBisCO assembly. Here, the crystal structure of RbcX from another cyanobacterium, Synechocystis sp. PCC6803, is reported, revealing an unusually long protruding C-terminal helix, as well as a bound polyethylene glycol molecule in the protein substrate-binding site.

PubMed: 17881829
DOI: 10.1107/S090744490704228X

実験手法

X-RAY DIFFRACTION (2.45 Å)