Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.
Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.
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DOI：
10.1021/acs.inorgchem.2c04490
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发表时间：
2023-05-01
影响因子：
4.6
通讯作者：
Subtilis, Bacillus
中科院分区：
文献类型：
--
作者：
Lee, Jaeick;Dalton, Rosemary A.;Basle, Arnaud;Vita, Nicolas;Dennison, Christopher;Subtilis, Bacillus
细菌铜储存蛋白（Csps）家族具有硫醇盐内衬的四螺旋束，其核心可以被Cu（I）离子填充。大多数Csps是胞质的（Csp3s），迄今为止进行的体外研究表明，来自发孢甲基弯菌OB3b（MtCsp3）、枯草芽孢杆菌（BsCsp3）和变铅青链霉菌（SlCsp3）的Csp3s是相似的。生物信息学已经突出了具有与这些表征的“经典”Csp3潜在不同的Cu（I）结合特性的同源物。本文测定了来自具有Cu（I）结合的甲烷氧化菌甲基囊藻属物种Rockwell菌株的蛋白质（RkCsp3）的晶体结构，将其鉴定为Csp3的新亚群的第一个研究实例。与经典Csp3s最显著的结构差异是在束的口处仅存在两个Cu（I）位点，Cu（I）离子通过所述位点进入和离开。这是由于缺少三个Cys残基和一个含His的基序，这使得经典的Csp3在该区域结合五到六个Cu（I）离子。无论如何，当使用高亲和力配体作为替代伴侣时，RkCsp3表现出快速的Cu（I）结合和Csp3的最快测量Cu（I）去除速率。对经典Csp3的新实验表明，它们的含His基序对于快速Cu（I）吸收和去除不是必需的。其他结构特征，可能是重要的，这些功能相关的体外性能进行了讨论。研究了影响胞质四螺旋束铜储存蛋白（Csp3s）功能的结构特征。一个新的Csp3亚家族成员的晶体结构定义了序列变化如何影响Cu（I）位点的数量和配位。的存在和位置的His配体周围的捆绑和协调的嘴和主核心之间的界面上的Cu（I）的结合和去除的残留物的影响进行了讨论。
A family of bacterial copper storage proteins (the Csps) possess thiolate-lined four-helix bundles whose cores can be filled with Cu(I) ions. The majority of Csps are cytosolic (Csp3s), and in vitro studies carried out to date indicate that the Csp3s from Methylosinus trichosporium OB3b (MtCsp3), Bacillus subtilis (BsCsp3), and Streptomyces lividans (SlCsp3) are alike. Bioinformatics have highlighted homologues with potentially different Cu(I)-binding properties from these characterized “classical” Csp3s. Determination herein of the crystal structure of the protein (RkCsp3) from the methanotroph Methylocystis sp. strain Rockwell with Cu(I) bound identifies this as the first studied example of a new subgroup of Csp3s. The most significant structural difference from classical Csp3s is the presence of only two Cu(I) sites at the mouth of the bundle via which Cu(I) ions enter and leave. This is due to the absence of three Cys residues and a His-containing motif, which allow classical Csp3s to bind five to six Cu(I) ions in this region. Regardless, RkCsp3 exhibits rapid Cu(I) binding and the fastest measured Cu(I) removal rate for a Csp3 when using high-affinity ligands as surrogate partners. New experiments on classical Csp3s demonstrate that their His-containing motif is not essential for fast Cu(I) uptake and removal. Other structural features that could be important for these functionally relevant in vitro properties are discussed. Structural features influencing the functionality of cytosolic four-helix bundle copper storage proteins (Csp3s) have been investigated. The crystal structure of a new Csp3 subfamily member defines how sequence variations can influence the number and coordination of Cu(I) sites. The impact of the presence and location of His ligands around the mouth of the bundle and a coordinating residue at the interface between the mouth and the main core on Cu(I) binding and removal is discussed.
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DOI：
10.1002/anie.201703107
发表时间：
2017-07-17
期刊：
Angewandte Chemie (International ed. in English)
影响因子：
--
作者：
Baslé A;Platsaki S;Dennison C
通讯作者：
Dennison C
DOI：
10.1107/s0907444905036693
发表时间：
2006-01-01
影响因子：
2.2
作者：
Evans, P
通讯作者：
Evans, P
影响因子：
2.3
作者：
Chino, Marco;Maglio, Ornella;Nastri, Flavia;Pavone, Vincenzo;DeGrado, William F.;Lombardi, Angela
通讯作者：
Lombardi, Angela
影响因子：
15
作者：
Bagchi P;Morgan MT;Bacsa J;Fahrni CJ
通讯作者：
Fahrni CJ
DOI：
10.1073/pnas.0802928105
发表时间：
2008-08-12
影响因子：
11.1
作者：
Hussain, Faiza;Olson, John S.;Wittung-Stafshede, Pernilla
通讯作者：
Wittung-Stafshede, Pernilla