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.

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.
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来自嗜热栖热菌 HB8 的假设蛋白 TTHA0829 的晶体结构,由胱硫醚-β-合酶 (CBS) 和天冬氨酸激酶分支酸变位酶 tyrA (ACT) 结构域组成。

DOI:
10.1007/s00792-016-0817-y
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发表时间:
2016
期刊:
影响因子:
2.9
通讯作者:
Kuramitsu S. and Higuchi Y.
Kuramitsu S. and Higuchi Y.
中科院分区:
生物学3区
文献类型:
--
作者:
Nakabayashi M.;Shibata N.;Ishido-Nakai E.;Kanagawa M.;Iio Y.;Komori H.;Ueda Y.;Nakagawa N.;Kuramitsu S. and Higuchi Y.

文献摘要

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来自thermus thermophilusHB8的TTHA0829分子质量为22,754 Da,由210个氨基酸残基组成。TTHA0829的表达在对数生长期后半段显著升高。TTHA0829可以形成四聚体或二聚体结构,主链折叠提供了n端半胱甘氨酸-β-合成酶(CBS)结构域和c端天冬氨酸激酶chorisate -mutase tyrA (ACT)结构域。CBS和ACT都是小配体分子可以结合的调节结构域。CBS结构域存在于所有生物的蛋白质中,通常为两个或四个串联拷贝。该结构域被认为是具有调节功能的小细胞内模块,通常位于几种酶和整体膜蛋白的活性(或功能)位点附近。ACT结构域在细胞内小分子结合结构域的βαββ - β- β- β基序列中包含4条β-链和2条α-螺旋,这些结构域有助于控制代谢、溶质转运和信号转导。我们根据TTHA0829的结构和表达模式来讨论其可能的作用。结果表明,TTHA0829作为细胞应激传感器或代谢物受体。
TTHA0829 fromThermus thermophilusHB8 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.