3EWK

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

3EWK の概要

• エントリーDOI: 10.2210/pdb3ewk/pdb
• 分子名称: Sensor protein, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: pas domain, alpha/beta fold, kinase, phosphoprotein, transferase, flavoprotein
• 由来する生物種: Methylococcus capsulatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26464.80

構造登録者

Ukaegbu, U.E.,Rosenzweig, A.C. (登録日: 2008-10-15, 公開日: 2009-03-24, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.34 Å)