3EWK

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

Summary for 3EWK

• Entry DOI: 10.2210/pdb3ewk/pdb
• Descriptor: Sensor protein, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: pas domain, alpha/beta fold, kinase, phosphoprotein, transferase, flavoprotein
• Biological source: Methylococcus capsulatus
• Total number of polymer chains: 1
• Total formula weight: 26464.80

Authors

Ukaegbu, U.E.,Rosenzweig, A.C. (deposition date: 2008-10-15, release date: 2009-03-24, Last modification date: 2023-12-27)

Primary citation

Ukaegbu, U.E.,Rosenzweig, A.C.
Structure of the Redox Sensor Domain of Methylococcus capsulatus (Bath) MmoS.
Biochemistry, 48:2207-2215, 2009

PubMed 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 A resolution. Both domains adopt the typical PAS domain alpha/beta topology and are structurally similar. The two domains are linked by a long alpha 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.

PubMed: 19271777
DOI: 10.1021/bi8019614

Experimental method

X-RAY DIFFRACTION (2.34 Å)