Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-β-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains

Makoto Nakabayashi, Naoki Shibata, Emi Ishido-Nakai, Mayumi Kanagawa, Yota Iio, Hirofumi Komori, Yasufumi Ueda, Noriko Nakagawa, Seiki Kuramitsu, Yoshiki Higuchi

Research output: Contribution to journalArticle

Abstract

TTHA0829 from Thermus thermophilus HB8 has a molecular mass of 22,754 Da and is composed of 210 amino acid residues. The expression of TTHA0829 is remarkably elevated in the latter half of logarithmic growth phase. TTHA0829 can form either a tetrameric or dimeric structure, and main-chain folding provides an N-terminal cystathionine-β-synthase (CBS) domain and a C-terminal aspartate-kinase chorismate-mutase tyrA (ACT) domain. Both CBS and ACT are regulatory domains to which a small ligand molecule can bind. The CBS domain is found in proteins from organisms belonging to all kingdoms and is observed frequently as two or four tandem copies. This domain is considered as a small intracellular module with a regulatory function and is typically found adjacent to the active (or functional) site of several enzymes and integral membrane proteins. The ACT domain comprises four β-strands and two α-helices in a βαββαβ motif typical of intracellular small molecule binding domains that help control metabolism, solute transport and signal transduction. We discuss the possible role of TTHA0829 based on its structure and expression pattern. The results imply that TTHA0829 acts as a cell-stress sensor or a metabolite acceptor.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalExtremophiles
DOIs
Publication statusAccepted/In press - Mar 3 2016

Fingerprint

Chorismate Mutase
Aspartate Kinase
Cystathionine
Thermus thermophilus
Proteins
Signal Transduction
Membrane Proteins
Ligands
Amino Acids
Enzymes
Growth

Keywords

  • ACT domain
  • CBS domain
  • Crystal structure
  • Gene-annotation
  • Hypothetical protein
  • Thermus thermophilus HB8

ASJC Scopus subject areas

  • Molecular Medicine
  • Microbiology

Cite this

Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-β-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains. / Nakabayashi, Makoto; Shibata, Naoki; Ishido-Nakai, Emi; Kanagawa, Mayumi; Iio, Yota; Komori, Hirofumi; Ueda, Yasufumi; Nakagawa, Noriko; Kuramitsu, Seiki; Higuchi, Yoshiki.

In: Extremophiles, 03.03.2016, p. 1-8.

Research output: Contribution to journalArticle

Nakabayashi, Makoto ; Shibata, Naoki ; Ishido-Nakai, Emi ; Kanagawa, Mayumi ; Iio, Yota ; Komori, Hirofumi ; Ueda, Yasufumi ; Nakagawa, Noriko ; Kuramitsu, Seiki ; Higuchi, Yoshiki. / Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-β-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains. In: Extremophiles. 2016 ; pp. 1-8.
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abstract = "TTHA0829 from Thermus thermophilus HB8 has a molecular mass of 22,754 Da and is composed of 210 amino acid residues. The expression of TTHA0829 is remarkably elevated in the latter half of logarithmic growth phase. TTHA0829 can form either a tetrameric or dimeric structure, and main-chain folding provides an N-terminal cystathionine-β-synthase (CBS) domain and a C-terminal aspartate-kinase chorismate-mutase tyrA (ACT) domain. Both CBS and ACT are regulatory domains to which a small ligand molecule can bind. The CBS domain is found in proteins from organisms belonging to all kingdoms and is observed frequently as two or four tandem copies. This domain is considered as a small intracellular module with a regulatory function and is typically found adjacent to the active (or functional) site of several enzymes and integral membrane proteins. The ACT domain comprises four β-strands and two α-helices in a βαββαβ motif typical of intracellular small molecule binding domains that help control metabolism, solute transport and signal transduction. We discuss the possible role of TTHA0829 based on its structure and expression pattern. The results imply that TTHA0829 acts as a cell-stress sensor or a metabolite acceptor.",
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AU - Nakabayashi, Makoto

AU - Shibata, Naoki

AU - Ishido-Nakai, Emi

AU - Kanagawa, Mayumi

AU - Iio, Yota

AU - Komori, Hirofumi

AU - Ueda, Yasufumi

AU - Nakagawa, Noriko

AU - Kuramitsu, Seiki

AU - Higuchi, Yoshiki

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