3Q20

Crystal structure of RbcX C103A mutant from Thermosynechococcus elongatus

「3KA1」から置き換えられました

3Q20 の概要

• エントリーDOI: 10.2210/pdb3q20/pdb
• 分子名称: RbcX protein, ACETATE ION, HEXANE-1,6-DIOL, ... (4 entities in total)
• 機能のキーワード: helix bundle, chaperone, rubisco assembly
• 由来する生物種: Thermosynechococcus elongatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29499.17

構造登録者

Tarnawski, M.,Krzywda, S.,Szczepaniak, A.,Jaskolski, M. (登録日: 2010-12-19, 公開日: 2011-01-26, 最終更新日: 2023-11-01)

主引用文献

Tarnawski, M.,Krzywda, S.,Bialek, W.,Jaskolski, M.,Szczepaniak, A.
Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus
Acta Crystallogr.,Sect.F, 67:851-857, 2011

PubMed Abstract: The crystal structure of TeRbcX, a RuBisCO assembly chaperone from the cyanobacterium Thermosynechococcus elongatus, a thermophilic organism, has been determined at 1.7 Å resolution. TeRbcX has an unusual cysteine residue at position 103 that is not found in RbcX proteins from mesophilic organisms. Unlike wild-type TeRbcX, a mutant protein with Cys103 replaced by Ala (TeRbcX-C103A) could be readily crystallized. The structure revealed that the overall fold of the TeRbcX homodimer is similar to those of previously crystallized RbcX proteins. Normal-mode analysis suggested that TeRbcX might adopt an open or closed conformation through a hinge movement pivoted on a kink in two long α4 helices. This type of conformational transition is presumably connected to RbcL (the large RuBisCO subunit) binding during the chaperone function of the RuBisCO assembly.

PubMed: 21821880
DOI: 10.1107/S1744309111018860

実験手法

X-RAY DIFFRACTION (1.71 Å)