Insight into Metal Removal from Peptides that Sequester Copper for Methane Oxidation.

Insight into Metal Removal from Peptides that Sequester Copper for Methane Oxidation.
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DOI:
10.1002/chem.201706035
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发表时间:
2018-03-26
期刊:
Chemistry (Weinheim an der Bergstrasse, Germany)
影响因子:
--
通讯作者:
Dennison C
Dennison C
中科院分区:
其他
文献类型:
--
作者:
Baslé A;El Ghazouani A;Lee J;Dennison C

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甲烷氧化菌素(Methanobactins,Mbns)是一种修饰的肽,其螯合甲烷氧化菌用于氧化甲烷的铜(Cu)。对于这类天然产物的结构信息有限,就像对细胞如何利用结合有Mn的Cu的理解一样。Methylosinus sporium NR 3 K CuI-Mbn的晶体结构提供了有关Mbns结构多样性的进一步信息,并首次深入了解了其Cu释放机制。来自恶唑酮和吡嗪二醇环的氮配体与来自硫代酰胺的相邻配位硫沿着螯合CuI。体外溶液数据与先前表征的Mbns中发现的CuI-Mbn单体一致。在晶体结构中,N-末端区域经历了构象变化,允许形成CuI 2-Mbn 2二聚体,其中CuI位点被来自相邻链的螯合单元结合。这样的结构改变将促进CuI从Mbns释放。
Methanobactins (Mbns) are modified peptides that sequester copper (Cu) methanotrophs use to oxidize methane. Limited structural information is available for this class of natural products, as is an understanding of how cells are able to utilize Mbn‐bound Cu. The crystal structure of Methylosinus sporium NR3K CuI–Mbn provides further information about the structural diversity of Mbns and the first insight into their Cu‐release mechanism. Nitrogen ligands from oxazolone and pyrazinediol rings chelate CuI along with adjacent coordinating sulfurs from thioamides. In vitro solution data are consistent with a CuI–Mbn monomer as found for previously characterized Mbns. In the crystal structure, the N‐terminal region has undergone a conformational change allowing the formation of a CuI 2–Mbn2 dimer with CuI sites bound by chelating units from adjacent chains. Such a structural alteration will facilitate CuI release from Mbns.
从甲基孢子菌素OB3b和甲基囊肿菌株SB2中的甲烷素的比较预测甲烷酰胺是由经过修饰的各种肽前体合成的,以创建一种用于结合和还原铜离子的共同核心。
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