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TitleStructure and mechanism of the alkane-oxidizing enzyme AlkB.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2180, Year 2023
Publish dateApr 17, 2023
AuthorsXue Guo / Jianxiu Zhang / Lei Han / Juliet Lee / Shoshana C Williams / Allison Forsberg / Yan Xu / Rachel Narehood Austin / Liang Feng /
PubMed AbstractAlkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase ...Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.
External linksNat Commun / PubMed:37069165 / PubMed Central
MethodsEM (single particle)
Resolution3.59 Å
Structure data

40303

8sbb

EMDB-40303, PDB-8sbb:
Cryo-EM structure of FtAlkB
Method: EM (single particle) / Resolution: 3.59 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-D12:
DODECANE

Source
  • fontimonas thermophila (bacteria)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / Enzyme

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