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 journalArticle

2 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 languageEnglish
Pages (from-to)265-271
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume430
Issue number1
DOIs
Publication statusPublished - 2013 Jan 4

Fingerprint

Cystathionine
Arabidopsis Proteins
Thioredoxins
Crystal structure
Adenosine Monophosphate
Arabidopsis
Dimers
Oxidation-Reduction
Monomers
Ligands
Proteins
Arabidopsis CDCP2 protein

Keywords

  • Arabidopsis thaliana
  • CBSX1
  • CBSX2
  • Cystathionine β-synthase domain
  • Plant
  • Thioredoxin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of the single cystathionine β-synthase domain-containing protein CBSX1 from Arabidopsis thaliana. / Jeong, Byung Cheon; Park, Si Hoon; Yoo, Kyoung Shin; Shin, Jeong Sheop; Song, Hyun Kyu.

In: Biochemical and Biophysical Research Communications, Vol. 430, No. 1, 04.01.2013, p. 265-271.

Research output: Contribution to journalArticle

@article{b47d3fee29d94b8397362857ff3d9955,
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}",
year = "2013",
month = "1",
day = "4",
doi = "10.1016/j.bbrc.2012.10.139",
language = "English",
volume = "430",
pages = "265--271",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "1",

}

TY - JOUR

T1 - Crystal structure of the single cystathionine β-synthase domain-containing protein CBSX1 from Arabidopsis thaliana

AU - Jeong, Byung Cheon

AU - Park, Si Hoon

AU - Yoo, Kyoung Shin

AU - Shin, Jeong Sheop

AU - Song, Hyun Kyu

PY - 2013/1/4

Y1 - 2013/1/4

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.

AB - 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.

KW - Arabidopsis thaliana

KW - CBSX1

KW - CBSX2

KW - Cystathionine β-synthase domain

KW - Plant

KW - Thioredoxin

UR - http://www.scopus.com/inward/record.url?scp=84872417277&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84872417277&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2012.10.139

DO - 10.1016/j.bbrc.2012.10.139

M3 - Article

C2 - 23159611

AN - SCOPUS:84872417277

VL - 430

SP - 265

EP - 271

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 1

ER -