High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A Fourier-transform infrared spectroscopic study

Andrea Scire; Emilia Pedone; Alessio Ausili; Michele Saviano; Maurizio Baldassarre; Enrico Bertoli; Simonetta Bartolucci; Fabio Tanfani

首页> 外文期刊>Molecular BioSystems >High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A Fourier-transform infrared spectroscopic study

【24h】

High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A Fourier-transform infrared spectroscopic study

机译：高静水压力引起的超嗜热古细菌火球菌蛋白质二硫键氧化还原酶的构象变化。傅立叶变换红外光谱研究

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

Protein disulfide oxidoreductases (PDOs) are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions. PDOs have been well studied in bacteria and eukarya, and they have been described in a number of thermophilic and hyperthermophilic species, where they play a critical role in the structural stabilization of intracellular proteins. In this study, the effect of high hydrostatic pressure on the structural properties of PDO from the hyperthermophilic archaeon Pyrococcus furiosus (PfPDO) was analysed in order to gain insights on the possible mechanisms used to endure extreme environmental conditions. The protein is highly thermostable and the data indicate that PfPDO is highly piezostable as well, and that different areas of the protein have a different local compressibility and resistance to high hydrostatic pressure. In particular, the results show that a-helices are more sensitive to pressure up to 5 kbar, whilst within 5-9 kbar the loss of P-sheets is more pronounced than the loss of a-helices. Examination of the PfPDO structure and calculations of the solvent accessible surface areas for each amino acid indicate that 42% of the PfPDO residues are buried and that the protein contains four small internal hydrophobic cavities. These findings are discussed in terms of important factors contributing to the high piezostability and thermostability of the enzyme.

机译：蛋白质二硫键氧化还原酶（PDO）是普遍存在的氧化还原酶，可催化二硫醇-二硫键交换反应。 PDO已在细菌和真核生物中进行了深入研究，并且已在许多嗜热和超嗜热物种中得到描述，它们在细胞内蛋白质的结构稳定中起关键作用。在这项研究中，分析了高静水压力对来自超嗜热古生火球菌（PfPDO）的PDO的结构特性的影响，以便深入了解用于忍受极端环境条件的可能机制。该蛋白质是高度热稳定的，数据表明PfPDO也是高度压电的，并且蛋白质的不同区域具有不同的局部可压缩性和对高静水压力的抵抗力。特别地，结果表明，α-螺旋对高达5kbar的压力更敏感，而在5-9kbar内，P-片的损失比α-螺旋的损失更为明显。对每个氨基酸的PfPDO结构检查和溶剂可及表面积的计算表明，有42％的PfPDO残基被掩埋，并且该蛋白质包含四个小的内部疏水腔。将根据有助于该酶的高压电稳定性和热稳定性的重要因素来讨论这些发现。

著录项

来源
《Molecular BioSystems》 |2010年第10期|p.2015-2022|共8页
作者
Andrea Scire; Emilia Pedone; Alessio Ausili; Michele Saviano; Maurizio Baldassarre; Enrico Bertoli; Simonetta Bartolucci; Fabio Tanfani;
展开▼
作者单位

Dipartimento di Biochimica, Biologia, e Genetica,Universita Politecnica delle Marche, Ancona, Italy;

rnIstituto di Biostrutiure e Bioimmagini, IBB-CNR,Via Mezzocannone 16, 80134 Napoli, Italy;

Departamento de Bioquimica y Biologia Molecular (A),Facultad de Veterinaria, Universidad de Murcia, Murcia, Spain;

rnIstituto di Biostrutiure e Bioimmagini, IBB-CNR,Via Mezzocannone 16, 80134 Napoli, Italy Dipartimento di Biologia Strutturale e Funzionale,Universitd degli Studi di Napoli 'Federico II', Napoli, Italy;

rnDipartimento di Biochimica, Biologia, e Genetica,Universita Politecnica delle Marche, Ancona, Italy;

rnDipartimento di Biochimica, Biologia, e Genetica,Universita Politecnica delle Marche, Ancona, Italy;

rnDipartimento di Biologia Strutturale e Funzionale,Universitd degli Studi di Napoli 'Federico II', Napoli, Italy;

rnDipartimento di Biochimica, Biologia, e Genetica,Universita Politecnica delle Marche, Ancona, Italy;

展开▼
收录信息
原文格式 PDF
正文语种 eng
中图分类
关键词

相似文献

外文文献
中文文献
专利

1. Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: a dynamic simulation and fourier transform infrared spectroscopic study. [J] . Pedone E, Saviano M, Bartolucci S, Journal of proteome research . 2005,第6期

机译：温度，SDS和pH诱导古细菌热球菌蛋白质二硫键氧化还原酶的构象变化：动态模拟和傅里叶变换红外光谱研究。
2. A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii [J] . Kashima Y., Ishikawa K. Archives of Biochemistry and Biophysics . 2003,第2期

机译：超级嗜热古生火球菌的硫氧还蛋白还原酶可还原一种超耐热的新型蛋白质-二硫键氧化还原酶
3. Proteome-wide prediction of novel DNA/RNA-binding proteins using amino acid composition and periodicity in the hyperthermophilic archaeon Pyrococcus furiosus. [J] . Fujishima K, Komasa M, Kitamura S, DNA research: an international journal for rapid publication of reports on genes and genomes . 2007,第3期

机译：在超嗜热古生火球菌中使用氨基酸组成和周期性预测蛋白质组范围内的新型DNA / RNA结合蛋白。
4. New Approaches Detection Secondary Conformation of Prion Protein in Frozen-Section Tissue by Fourier-Transform Infrared Microscopy [C] . Norio Miyoshi, Hiroyuki Okada, Masuhiro Takata, Conference on New Approaches in Biomedical Spectroscopy . 2007

机译：傅立叶变换红外显微镜，新方法检测冷冻截面组织中朊病毒蛋白的二次构象
5. Investigations into the enzymology and biotechnology of the hyperthermophilic carboxypeptidase (PfuCP) from the archaeon Pyrococcus furiosus. [D] . Cheng, Timothy Casey. 2003

机译：古生热球菌嗜热型羧肽酶（PfuCP）的酶学和生物技术研究。
6. Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus. [O] . Corné H Verhees, Denise G M Koot, Thijs J G Ettema, 2002

机译：来自超嗜热古生热球菌的两种糖激酶的生化适应性。
7. The purificarion, cloning, and high level expression of a glutaredoxin-like protein from the hyperthermophilic Archaeon Pyrococcus furiosus. [O] . GUAGLIARDI A., CANNIO R., DE PASCALE D., 1995

机译：从超嗜热古菌pyrococcus furiosus中纯化，克隆和高水平表达谷氧还蛋白样蛋白。

High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A Fourier-transform infrared spectroscopic study

摘要

著录项

相似文献

相关主题

期刊订阅