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TitleStructural basis for enzymatic terminal C-H bond functionalization of alkanes.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 4, Page 521-526, Year 2023
Publish dateMar 30, 2023
AuthorsJin Chai / Gongrui Guo / Sean M McSweeney / John Shanklin / Qun Liu /
PubMed AbstractAlkane monooxygenase (AlkB) is a widely occurring integral membrane metalloenzyme that catalyzes the initial step in the functionalization of recalcitrant alkanes with high terminal selectivity. AlkB ...Alkane monooxygenase (AlkB) is a widely occurring integral membrane metalloenzyme that catalyzes the initial step in the functionalization of recalcitrant alkanes with high terminal selectivity. AlkB enables diverse microorganisms to use alkanes as their sole carbon and energy source. Here we present the 48.6-kDa cryo-electron microscopy structure of a natural fusion from Fontimonas thermophila between AlkB and its electron donor AlkG at 2.76 Å resolution. The AlkB portion contains six transmembrane helices with an alkane entry tunnel within its transmembrane domain. A dodecane substrate is oriented by hydrophobic tunnel-lining residues to present a terminal C-H bond toward a diiron active site. AlkG, an [Fe-4S] rubredoxin, docks via electrostatic interactions and sequentially transfers electrons to the diiron center. The archetypal structural complex presented reveals the basis for terminal C-H selectivity and functionalization within this broadly distributed evolutionary class of enzymes.
External linksNat Struct Mol Biol / PubMed:36997762 / PubMed Central
MethodsEM (single particle)
Resolution2.76 Å
Structure data

28890

8f6t

EMDB-28890, PDB-8f6t:
Cryo-EM structure of alkane 1-monooxygenase AlkB-AlkG complex from Fontimonas thermophila
Method: EM (single particle) / Resolution: 2.76 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-D12:
DODECANE

Source
  • fontimonas thermophila (bacteria)
KeywordsOXIDOREDUCTASE / Electron transfer complex / iron-sulfur cluster / histidine-diiron center / hydrophobic alkane binding pocket

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