A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
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DOI：
10.1016/j.jinorgbio.2014.07.022
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发表时间：
2014-11-01
影响因子：
3.9
通讯作者：
Soncini, Fernando C.
中科院分区：
文献类型：
--
作者：
Abriata, Luciano A.;Pontel, Lucas B.;Soncini, Fernando C.
CueP 通过未知机制赋予细菌周质铜抗性，特别是在厌氧条件下。唯一可用的结构和有限的溶液数据表明 CueP 在溶液中形成非共价定时器，而序列保守表明三个半胱氨酸和两个组氨酸作为铜配体的重要作用。在这里，我们报告了由新发现的功能相关界面介导的二聚平衡的证据，该界面封闭了内部铜位点和二硫键，但允许链内和链间二硫键键合、广泛的二硫键中继和界面铜位点。我们的结果表明 CueP 在氧化还原态传感和铜解毒之间发挥着重要作用。 (C) 2014 Elsevier Inc. 保留所有权利。
CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent timers in solution, whereas sequence conservation suggests important roles for three cysteines and two histidines as copper ligands. Here we report evidence of a dimerization equilibrium mediated by a newly identified interface of functional relevance, which occludes internal copper sites and disulfide bonds but allows for intra- and interchain disulfide bonding, an extensive disulfide relay, and interfacial copper sites. Our results suggest a role for CueP linking redox-state sensing and copper detoxification. (C) 2014 Elsevier Inc. All rights reserved.