Structure of the redox sensor domain of methylococcus capsulatus (bath) MmoS

Uchechi E. Ukaegbu, Amy C Rosenzweig

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

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 those of 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.

Original languageEnglish (US)
Pages (from-to)2207-2215
Number of pages9
JournalBiochemistry
Volume48
Issue number10
DOIs
StatePublished - Mar 17 2009

ASJC Scopus subject areas

  • Biochemistry

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