Change in single cystathionine β-synthase domain-containing protein from a bent to flat conformation upon adenosine monophosphate binding

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

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Cystathionine β-synthase (CBS) domains are small intracellular modules that can act as binding domains for adenosine derivatives, and they may regulate the activity of associated enzymes or other functional domains. Among these, the single CBS domain-containing proteins, CBSXs, from Arabidopsis thaliana, have recently been identified as redox regulators of the thioredoxin system. Here, the crystal structure of CBSX2 in complex with adenosine monophosphate (AMP) is reported at 2.2. Å resolution. The structure of dimeric CBSX2 with bound-AMP is shown to be approximately flat, which is in stark contrast to the bent form of apo-CBSXs. This conformational change in quaternary structure is triggered by a local structural change of the unique α5 helix, and by moving each loop P into an open conformation to accommodate incoming ligands. Furthermore, subtle rearrangement of the dimer interface triggers movement of all subunits, and consequently, the bent structure of the CBSX2 dimer becomes a flat structure. This reshaping of the structure upon complex formation with adenosine-containing ligand provides evidence that ligand-induced conformational reorganization of antiparallel CBS domains is an important regulatory mechanism.

Original languageEnglish
Pages (from-to)40-46
Number of pages7
JournalJournal of Structural Biology
Volume183
Issue number1
DOIs
Publication statusPublished - 2013 Jul 1

Fingerprint

Cystathionine
Adenosine Monophosphate
Ligands
Adenosine
Arabidopsis Proteins
Thioredoxins
Oxidation-Reduction
Enzymes
Protein Domains

Keywords

  • AMP
  • APA
  • Arabidopsis thaliana
  • Bateman domain
  • CBS
  • CBS domain
  • CBSX2
  • CDCP
  • Conformational change
  • Crystal structure
  • RMSD
  • SAM
  • Trx

ASJC Scopus subject areas

  • Structural Biology

Cite this

Change in single cystathionine β-synthase domain-containing protein from a bent to flat conformation upon adenosine monophosphate binding. / Jeong, Byung Cheon; Park, Si Hoon; Yoo, Kyoung Shin; Shin, Jeong Sheop; Song, Hyun Kyu.

In: Journal of Structural Biology, Vol. 183, No. 1, 01.07.2013, p. 40-46.

Research output: Contribution to journalArticle

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