Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS.

Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS.
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DOI:
10.1021/bi8019614
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发表时间:
2009-03-17
期刊:
影响因子:
2.9
通讯作者:
Rosenzweig, Amy C.
Rosenzweig, Amy C.
中科院分区:
生物学3区
文献类型:
--
作者:
Ukaegbu, Uchechi E.;Rosenzweig, Amy C.

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来自荚膜甲基球菌(Methylococcus capsulatus, Bath)的MmoS是一个双组分信号系统的多结构域传感器蛋白,被认为在铜介导的可溶性甲烷单加氧酶(sMMO)调控中发挥作用。MmoS在其n端串联per - art - sim (PAS)结构域内结合FAD辅因子,表明其具有氧化还原传感器的功能。MmoS串联PAS结构域的晶体结构,指定PAS- a和PAS- b,已被确定为2.34 Å分辨率。两个结构域均采用典型的PAS结构域α/β拓扑结构,结构相似。这两个结构域由一个长α螺旋连接,彼此不相互作用。FAD辅因子单独安置在PAS-A内,并通过扩展的氢键网络稳定。PAS- a的整体折叠与其他含黄素的PAS结构域相似,但在MmoS传感器中未观察到其他结构中的同二聚体相互作用,其结晶为单体。该结构既为串联PAS结构域的结构提供了新的见解,也提示了可能在MmoS、FAD氧化还原化学和随后的信号转导中发挥作用的特定残基。
MmoS from Methylococcus capsulatus (Bath) is the multidomain sensor protein of a two component signaling system proposed to play a role in the copper-mediated regulation of soluble methane monooxygenase (sMMO). MmoS binds an FAD cofactor within its N-terminal tandem Per-Arnt-Sim (PAS) domains, suggesting that it functions as a redox sensor. The crystal structure of the MmoS tandem PAS domains, designated PAS-A and PAS-B, has been determined to 2.34 Å resolution. Both domains adopt the typical PAS domain α/β topology and are structurally similar. The two domains are linked by a long α helix and do not interact with one another. The FAD cofactor is housed solely within PAS-A and is stabilized by an extended hydrogen bonding network. The overall fold of PAS-A is similar to other flavin-containing PAS domains, but homodimeric interactions in other structures are not observed in the MmoS sensor, which crystallized as a monomer. The structure both provides new insight into the architecture of tandem PAS domains and suggests specific residues that may play a role in MmoS FAD redox chemistry and subsequent signal transduction.
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