4GQV

Crystal structure of CBS-pair protein, CBSX1 from Arabidopsis thaliana

4GQV の概要

• エントリーDOI: 10.2210/pdb4gqv/pdb
• 関連するPDBエントリー: 4GQW
• 分子名称: CBS domain-containing protein CBSX1, chloroplastic (2 entities in total)
• 機能のキーワード: cbs domain, thioredoxin, chloroplast, plant, protein binding
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Plastid, chloroplast: O23193
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18226.81

構造登録者

Jeong, B.-C.,Park, S.H.,Yoo, K.S.,Shin, J.S.,Song, H.K. (登録日: 2012-08-24, 公開日: 2013-01-16, 最終更新日: 2024-03-20)

主引用文献

Jeong, B.C.,Park, S.H.,Yoo, K.S.,Shin, J.S.,Song, H.K.
Crystal structure of the single cystathionine beta-synthase domain-containing protein CBSX1 from Arabidopsis thaliana
Biochem.Biophys.Res.Commun., 430:265-271, 2013

PubMed Abstract: The single cystathionine β-synthase (CBS) pair proteins from Arabidopsis thaliana have been identified as being a redox regulator of the thioredoxin (Trx) system. CBSX1 and CBSX2, which are two of the six Arabidopsis cystathione β-synthase domain-containing proteins that contain only a single CBS pair, have close sequence similarity. Recently, the crystal structure of CBSX2 was determined and a significant portion of the internal region was disordered. In this study, crystal structures of full-length CBSX1 and the internal loop deleted (Δloop) form are reported at resolutions of 2.4 and 2.2Å, respectively. The structures of CBSX1 show that they form anti-parallel dimers along their central twofold axis and have a unique ∼155° bend along the side. This is different from the angle of CBSX2, which is suggestive of the flexible nature of the relative angle between the monomers. The biochemical data that were obtained using the deletion as well as point mutants of CBSX1 confirmed the importance of AMP-ligand binding in terms of enhancing Trx activity.

PubMed: 23159611
DOI: 10.1016/j.bbrc.2012.10.139

実験手法

X-RAY DIFFRACTION (2.392 Å)