Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus
Exploring the catalytic mechanism of the first dimeric Bcp: Functional, structural and docking analyses of Bcp4 from Sulfolobus solfataricus
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DOI：
10.1016/j.biochi.2010.07.006
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发表时间：
2010-10-01
期刊：
影响因子：
3.9
通讯作者：
Bartolucci, Simonetta
中科院分区：
文献类型：
--
作者：
Limauro, Danila;D'Ambrosio, Katia;Bartolucci, Simonetta
硫磺硫化叶菌中过氧化物的解毒作用是由细菌铁蛋白共迁移蛋白（Bcps）、Bcp 1（Sso 2071）、Bcp 2（Sso 2121）、Bcp 3（Sso 2255）和Bcp 4（Sso 2613）进行的，这些抗氧化酶属于过氧化物还原酶的一个亚家族。在本文中，我们报告的功能，结构和对接分析的Bcp 4，其特征在于在活性位点的CXXXXC基序。Bcp 4代表了迄今为止研究的第一个二聚体Bcp。生化研究表明，该蛋白具有非共价二聚体结构，并采用非典型的2-Cys催化机制。代表完全还原酶状态的双突变体C45 S/C50 S的X射线结构描述了蛋白质二聚体排列。最后，同时提供的晶体结构的单体Bcp 1允许比较分析的相互作用与蛋白质二硫化物氧化还原酶SsPDO（Sso 0192），参与减少Bcp 1和Bcp 4，通过蛋白质蛋白质对接的方法。(C)2010年Elsevier Masson SAS。All rights reserved.
The detoxification from peroxides in Sulfolobus solfataricus is performed by the Bacterioferritin comigratory proteins (Bcps), Bcp1 (Sso2071), Bcp2 (Sso2121), Bcp3 (Sso2255) and Bcp4 (Sso2613), antioxidant enzymes belonging to one of the subfamilies of the Peroxiredoxins. In this paper we report on the functional, structural and docking analyses of Bcp4, characterized by the CXXXXC motif in the active site. Bcp4 represents the first dimeric Bcp so far investigated. Biochemical studies showed that the protein has a non-covalent dimeric structure and adopts an atypical 2-Cys catalytic mechanism. The X-ray structure of the double mutant C45S/C50S, representative of the fully reduced enzyme state, described the protein dimeric arrangement. Finally, concurrent availability of the crystallographic structure of the monomeric Bcp1 allowed comparative analysis of the interaction with Protein Disulfide Oxidoreductase SsPDO (Sso0192), involved in the reduction of both Bcp1 and Bcp4, through a protein protein docking approach. (C) 2010 Elsevier Masson SAS. All rights reserved.