Heartbeat-like dynamics drives oxygen activation in methane monooxygenase
Hwang, Y.; Ryu, B.; Lee, D.-H.; Hong, H. J.; Na, J.-G.; Song, C. G.; Kang, H. G.; Pozharski, E.; Lee, S. J.
Show abstract
Soluble methane monooxygenase (sMMO) is an enzyme that hydroxylates methane (CH4), a potent greenhouse gas, at non-heme di-iron active sites under atmospheric conditions. The regulatory component (MMOB) is essential for the catalytic activity of hydroxylase (MMOH) as it induces conformational changes in the active site and facilitating substrate ingress. Recent advances in cryogenic electron microscopy (cryo-EM) have enabled us to elucidate the high resolution picture of sMMO catalytic mechanism. We describe the 2.85 [A] cryo-EM structure of MMOH-MMOB, with one equivalent of MMOB bound to MMOH (H-1B), which is in contrast with previously solved crystal structures. MMOB allosterically regulates the MMOH protomer ({beta}{gamma}) and induces conformational changes that propagate from the surface to the di-iron coordination site. The N-terminal region of the MMOH {beta}-subunit (NT-H{beta}) stabilizes helices essential for iron coordination and oxygen activation. The MMOB-bound protomer (HBA, {beta}{gamma}B) presents the first structural report of a 2.7 [A] Fe{middle dot}{middle dot}{middle dot}Fe distance, while the non-MMOB-bound protomer (HBB, {beta}{gamma}) and MMOH display a 3.1 [A] distance. The coordination of Fe-ligands is maintained by the structural stabilization provided by the {beta}- and {gamma}-subunits of MMOH. This novel cryo-EM structure reveals new coordination environments, offering crucial mechanistic insights into sMMO catalysis.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Structure of mycobacterial respiratory Complex I 96%
- Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium Deinococcus radiodurans 96%
- Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochrome c in the yeast III-IV respiratory supercomplex 96%
Similar papers in this journal
- Structural evidence for two-stage binding of mitochondrial ferredoxin 2 to the core iron-sulfur cluster assembly complex 96%
- Cryo-EM structures of Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae 96%
- Conformational Landscapes of a Class I Ribonucleotide Reductase Complex during Turnover Reveal Intrinsic Dynamics and Asymmetry 96%
Similar papers in this journal
- A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire 97%
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature 96%
- Structure and dynamics of Odinarchaeota tubulin and the implications for eukaryotic microtubule evolution 96%
Similar papers in this journal
- Structural basis for molecular assembly of fucoxanthin chlorophyll a/c-binding proteins in a diatom photosystem I supercomplex 95%
- Deciphering a hexameric protein complex with Angstrom optical resolution 94%
- The giant Mimivirus 1.2 Mb genome is elegantly organized into a 30 nm helical protein shield 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.