Crystal structure of the single cystathionine ¦Â-synthase domain-containing protein CBSX1 from Arabidopsis thaliana

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• 作者：Byung-Cheon Jeong^a ; Si Hoon Park^a ; Kyoung Shin Yoo^b ; Jeong Sheop Shin^a ; Hyun Kyu Song^a ; ^{hksong@korea.ac.kr}
• 关键词：CBS ; cystathionine ¦Â-synthase ; CDCP ; CBS domain-containing protein ; MR ; molecular replacement ; RMS ; root mean square ; TEV ; tobacco etch virus ; Trx ; thioredoxin
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2013
• 出版时间：4 January, 2013
• 年：2013
• 卷：430
• 期：1
• 页码：265-271
• 全文大小：1220 K

文摘

The single cystathionine ¦Â-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 ¦Â-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 (¦¤loop) form are reported at resolutions of 2.4 and 2.2 ?, respectively. The structures of CBSX1 show that they form anti-parallel dimers along their central twofold axis and have a unique ¡«155¡ã 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.