Methane monooxygenase

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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 />
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* Subunit γ is regulatory (MMOB) which is involved in coupling.<br />
+
* 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

Structure of methane monooxygenase α (grey and green) +β (pink and yellow) +γ (magenta and cyan) subunits complex with Fe+3 (red), Ca+2 (green) and dibromomethane (PDB code 1fz8).

Drag the structure with the mouse to rotate

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
  • 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
  • MMO γ subunit (MMO reductase, MMOR)
    • 1jq4 – McMMOR N terminal + Fe2S2 - NMR
    • 1tvc – McMMOR C terminal + FAD derivative - NMR

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References

  1. 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
  2. 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

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Michal Harel

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