c-di-AMP recognition by Staphylococcus aureus PstA
c-di-AMP recognition by Staphylococcus aureus PstA
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DOI：
10.1016/j.febslet.2014.11.022
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发表时间：
2015-01-02
期刊：
影响因子：
3.5
通讯作者：
Witte, Gregor
中科院分区：
文献类型：
--
作者：
Mueller, Martina;Hopfner, Karl-Peter;Witte, Gregor
环二腺苷酸（c-di-AMP）是细菌的第二信使，参与多种过程，包括DNA完整性、细胞壁代谢和钾离子转运。最近在金黄色葡萄球菌中鉴定了许多c-di-AMP受体蛋白。其中之一- PstA -具有铁氧还蛋白样折叠，并且在结构上与PII信号转导蛋白类相关。PII蛋白参与了大量的途径，其中大多数与氮代谢有关。在这项研究中，我们描述了模式的c-di-AMP的结合和随后的结构变化的S。金黄色葡萄球菌与经典PII蛋白相比，PstA中的改变的结构导致配体配位的差异。(C)2014年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Cyclic-di-AMP (c-di-AMP) is a bacterial secondary messenger involved in various processes, including sensing of DNA-integrity, cell wall metabolism and potassium transport. A number of c-di-AMP receptor proteins have recently been identified in Staphylococcus aureus. One of them - PstA - possesses a ferredoxin-like fold and is structurally related to the class of PII signal-transduction proteins. PII proteins are involved in a large number of pathways, most of them associated with nitrogen metabolism. In this study we describe the mode of c-di-AMP binding and subsequent structural changes of S. aureus PstA. An altered architecture in PstA compared to canonical PII proteins results in differences in ligand coordination. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.