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

Byung Cheon Jeong; Si Hoon Park; Kyoung Shin Yoo; Jeong Sheop Shin; Hyun Kyu Song

doi:10.1016/j.bbrc.2012.10.139

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

Byung Cheon Jeong, Si Hoon Park, Kyoung Shin Yoo, Jeong Sheop Shin, Hyun Kyu Song

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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 2.2. å, 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.

Original language	English
Pages (from-to)	265-271
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	430
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2012.10.139
Publication status	Published - 2013 Jan 4

Bibliographical note

Funding Information:
We thank the staff at AR-NW12A beamline, Photon Factory, Japan for helping us with the data collection. This work was supported by a National Research Foundation of Korea (NRF) grant that was funded by the Korean Government (MEST; 2011-0028168 ) and the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare & Family Affairs, Republic of Korea ( A092006 ).

Keywords

Arabidopsis thaliana
CBSX1
CBSX2
Cystathionine β-synthase domain
Plant
Thioredoxin

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2012.10.139

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title = "Crystal structure of the single cystathionine β-synthase domain-containing protein CBSX1 from Arabidopsis thaliana",

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 2.2. {\aa}, 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.",

keywords = "Arabidopsis thaliana, CBSX1, CBSX2, Cystathionine β-synthase domain, Plant, Thioredoxin",

author = "Jeong, {Byung Cheon} and Park, {Si Hoon} and Yoo, {Kyoung Shin} and Shin, {Jeong Sheop} and Song, {Hyun Kyu}",

note = "Funding Information: We thank the staff at AR-NW12A beamline, Photon Factory, Japan for helping us with the data collection. This work was supported by a National Research Foundation of Korea (NRF) grant that was funded by the Korean Government (MEST; 2011-0028168 ) and the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare & Family Affairs, Republic of Korea ( A092006 ).",

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AU - Shin, Jeong Sheop

AU - Song, Hyun Kyu

N1 - Funding Information: We thank the staff at AR-NW12A beamline, Photon Factory, Japan for helping us with the data collection. This work was supported by a National Research Foundation of Korea (NRF) grant that was funded by the Korean Government (MEST; 2011-0028168 ) and the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare & Family Affairs, Republic of Korea ( A092006 ).

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N2 - 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 2.2. å, 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.

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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