3d1c

Crystal structure of Flavin-containing Putative Monooxygenase (NP_373108.1) from STAPHYLOCOCCUS AUREUS MU50 at 2.40 A resolution

spinqualitylabelsall models 3d1c, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3d1c is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus Mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FAD, MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function A0A0H3JN45_STAAN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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