1YKW

Crystal Structure of a Novel RuBisCO-Like Protein from the Green Sulfur Bacterium Chlorobium tepidum

1YKW の概要

• エントリーDOI: 10.2210/pdb1ykw/pdb
• 分子名称: RuBisCO-like protein (2 entities in total)
• 機能のキーワード: beta-alpha-barrel, unknown function
• 由来する生物種: Chlorobaculum tepidum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96051.45

構造登録者

Li, H.,Sawaya, M.R.,Tabita, F.R.,Eisenberg, D. (登録日: 2005-01-18, 公開日: 2005-05-17, 最終更新日: 2023-08-23)

主引用文献

Li, H.,Sawaya, M.R.,Tabita, F.R.,Eisenberg, D.
Crystal structure of a RuBisCO-like protein from the green sulfur bacterium Chlorobium tepidum.
Structure, 13:779-789, 2005

PubMed Abstract: Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyzes the incorporation of atmospheric CO(2) into ribulose 1,5-bisphosphate (RuBP). RuBisCOs are classified into four forms based on sequence similarity: forms I, II and III are bona fide RuBisCOs; form IV, also called the RuBisCO-like protein (RLP), lacks several of the substrate binding and catalytic residues and does not catalyze RuBP-dependent CO(2) fixation in vitro. To contribute to understanding the function of RLPs, we determined the crystal structure of the RLP from Chlorobium tepidum. The overall structure of the RLP is similar to the structures of the three other forms of RuBisCO; however, the active site is distinct from those of bona fide RuBisCOs and suggests that the RLP is possibly capable of catalyzing enolization but not carboxylation. Bioinformatic analysis of the protein functional linkages suggests that this RLP coevolved with enzymes of the bacteriochlorophyll biosynthesis pathway and may be involved in processes related to photosynthesis.

PubMed: 15893668
DOI: 10.1016/j.str.2005.02.017

実験手法

X-RAY DIFFRACTION (2 Å)