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.
中科院分区:
文献类型:
--
作者:
Ukaegbu, Uchechi E.;Rosenzweig, Amy C.
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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