8SBB
Cryo-EM structure of FtAlkB
Summary for 8SBB
| Entry DOI | 10.2210/pdb8sbb/pdb |
| EMDB information | 40303 |
| Descriptor | Alkane 1-monooxygenase, Nanobody, FE (III) ION, ... (4 entities in total) |
| Functional Keywords | enzyme, membrane protein |
| Biological source | Fontimonas thermophila More |
| Total number of polymer chains | 2 |
| Total formula weight | 60353.54 |
| Authors | |
| Primary citation | Guo, X.,Zhang, J.,Han, L.,Lee, J.,Williams, S.C.,Forsberg, A.,Xu, Y.,Austin, R.N.,Feng, L. Structure and mechanism of the alkane-oxidizing enzyme AlkB. Nat Commun, 14:2180-2180, 2023 Cited by PubMed Abstract: 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. PubMed: 37069165DOI: 10.1038/s41467-023-37869-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.59 Å) |
Structure validation
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