8F6T

Cryo-EM structure of alkane 1-monooxygenase AlkB-AlkG complex from Fontimonas thermophila

Summary for 8F6T

• Entry DOI: 10.2210/pdb8f6t/pdb
• EMDB information: 28890
• Descriptor: Alkane 1-monooxygenase, FE (III) ION, DODECANE (3 entities in total)
• Functional Keywords: electron transfer complex, iron-sulfur cluster, histidine-diiron center, hydrophobic alkane binding pocket, oxidoreductase
• Biological source: Fontimonas thermophila
• Total number of polymer chains: 1
• Total formula weight: 53280.03

Authors

Chai, J.,Guo, G.,McSweeney, S.,Shanklin, J.,Liu, Q. (deposition date: 2022-11-17, release date: 2023-04-05, Last modification date: 2024-05-22)

Primary citation

Chai, J.,Guo, G.,McSweeney, S.M.,Shanklin, J.,Liu, Q.
Structural basis for enzymatic terminal C-H bond functionalization of alkanes.
Nat.Struct.Mol.Biol., 30:521-526, 2023

PubMed Abstract: 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.

PubMed: 36997762
DOI: 10.1038/s41594-023-00958-0

Experimental method

ELECTRON MICROSCOPY (2.76 Å)