Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Flavin-containing Monooxygenase (FMO) catalyzed the oxygenation of broad spectrum of substrates. FMO can also serve as biocatalysts in the Baeyer-Villiger reaction in organic synthesis. Here we report the high-resolution crystal structure of a Baeyer-Villiger Flavin-containing Monooxygenase (BVFMO) from methicillin- and vancomycin-resistant Staphylococcus aureus strain MU50. The structure of Staphylococcus aureus FMO should facilitate further development of BVFMO as biocatalysts. A possible role of Staphylococcus aureus FMO in methicillin and vancomycin resistance is discussed. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
Crystal structure of a Baeyer-Villiger Flavin-containing monooxygenase from Staphylococcus aureus MRSA strain MU50.,Hwang WC, Xu Q, Wu B, Godzik A Proteins. 2014 Aug 5. doi: 10.1002/prot.24661. PMID:25092800[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hwang WC, Xu Q, Wu B, Godzik A. Crystal structure of a Baeyer-Villiger Flavin-containing monooxygenase from Staphylococcus aureus MRSA strain MU50. Proteins. 2014 Aug 5. doi: 10.1002/prot.24661. PMID:25092800 doi:http://dx.doi.org/10.1002/prot.24661
