Methane monooxygenase
From Proteopedia
(Difference between revisions)
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* Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br /> | * Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br /> | ||
* Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | * Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | ||
- | * Subunit γ is regulatory (MMOB) | + | * Subunit γ is regulatory (MMOB) and is involved in coupling.<br /> |
MMO is found in methanotropic bacteria. | MMO is found in methanotropic bacteria. | ||
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**[[1xmg]] – McMMO α+β+γ subunits <br /> | **[[1xmg]] – McMMO α+β+γ subunits <br /> | ||
**[[1yew]], [[3rgb]] – McMMO α+β+γ subunits + Cu + Zn<br /> | **[[1yew]], [[3rgb]] – McMMO α+β+γ subunits + Cu + Zn<br /> | ||
- | **[[1mhy]], [[1mhz]] – MtMMO α+β+γ subunits + Fe – ''Methylosinus trichosporium''<br /> | + | **[[1mhy]], [[1mhz]], [[6vk5]], [[6vk6]], [[6vk7] – MtMMO α+β+γ subunits + Fe+3 – ''Methylosinus trichosporium''<br /> |
+ | **[[6vk4]] – MtMMO α+β+γ subunits + Fe+3 + Fe+2<br /> | ||
+ | **[[6vk8]] – MtMMO α+β+γ subunits + Fe+3 + succinate<br /> | ||
**[[6cxh]] – MMO α+β+γ subunits + Cu – ''Methylomicrobium alcaliphilum''<br /> | **[[6cxh]] – MMO α+β+γ subunits + Cu – ''Methylomicrobium alcaliphilum''<br /> | ||
Revision as of 09:43, 6 September 2020
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3D structures of methane monooxygenase
Updated on 06-September-2020 {{#tree:id=OrganizedByTopic|openlevels=0|
- Methane monooxygenase
- 1mmo, 1mty, 1fyz, 1fz0, 1fz1, 1fz2, 1fz3, 1fz4, 1fz5, 1fz6, 1fz7, 1fzh, 1fzi, 1xu5 – McMMO α+β+γ subunits + Fe – Methylococcus capsulatus
- 1xmf – McMMO α+β+γ subunits + Mn
- 1xmh – McMMO α+β+γ subunits + Co
- 1xmg – McMMO α+β+γ subunits
- 1yew, 3rgb – McMMO α+β+γ subunits + Cu + Zn
- 1mhy, 1mhz, 6vk5, 6vk6, [[6vk7] – MtMMO α+β+γ subunits + Fe+3 – Methylosinus trichosporium
- 6vk4 – MtMMO α+β+γ subunits + Fe+3 + Fe+2
- 6vk8 – MtMMO α+β+γ subunits + Fe+3 + succinate
- 6cxh – MMO α+β+γ subunits + Cu – Methylomicrobium alcaliphilum
- 1mmo, 1mty, 1fyz, 1fz0, 1fz1, 1fz2, 1fz3, 1fz4, 1fz5, 1fz6, 1fz7, 1fzh, 1fzi, 1xu5 – McMMO α+β+γ subunits + Fe – Methylococcus capsulatus
- MMO complexes
- 1fz8 – McMMO α+β+γ subunits + Fe + dibromomethane
- 1xvc – McMMO α+β+γ subunits + Fe + bromoethane + bromopentane
- 1xvb – McMMO α+β+γ subunits + Fe + bromoethane + bromopropane + bromobutane + bromohexanol
- 1fz9 – McMMO α+β+γ subunits + Fe + iodoethane
- 1xvd – McMMO α+β+γ subunits + Fe + fluorophenol
- 1xve – McMMO α+β+γ subunits + Fe + bromobutenol
- 1xvf – McMMO α+β+γ subunits + Fe + chloropropanol
- 1xvg – McMMO α+β+γ subunits + Fe + bromoethanol
- 1xu3 – McMMO α+β+γ subunits + Fe + bromophenol
- 4gam – McMMO α+β+γ subunits + Fe + MMO regulatory protein B
- 4phz, 4pi0 – MeMMO α+β+γ subunits + Cu + peptide - methylocystis
- 4pi2 – MeMMO α+β+γ subunits + Cu + Zn + peptide
- 1fz8 – McMMO α+β+γ subunits + Fe + dibromomethane
- MMO γ subunit (MMO reductase, MMOR)
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References
- ↑ Lipscomb JD. Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol. 1994;48:371-99. PMID:7826011 doi:http://dx.doi.org/10.1146/annurev.mi.48.100194.002103
- ↑ Miyaji A. Particulate methane monooxygenase from Methylosinus trichosporium OB3b. Methods Enzymol. 2011;495:211-25. doi: 10.1016/B978-0-12-386905-0.00014-0. PMID:21419924 doi:http://dx.doi.org/10.1016/B978-0-12-386905-0.00014-0