7byu

Crystal structure of Acidovorax avenae L-fucose mutarotase (apo form)

spinqualitylabelsall models 7byu, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7byu is a 2 chain structure with sequence from Acidovorax avenae subsp. avenae ATCC 19860. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.206Å Ligands: 1PG, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F0Q4R9_ACIAP Publication Abstract from PubMed Mutarotases catalyze the alpha-beta anomeric conversion of monosaccharide, and play a key role in utilizing sugar as enzymes involved in sugar metabolism have specificity for the alpha- or beta-anomer. In spite of the sequential similarity to l-rhamnose mutarotase protein superfamily (COG3254: RhaM), the ACAV_RS08160 gene in Acidovorax avenae ATCC 19860 (AaFucM) is located in a gene cluster related to non-phosphorylative l-fucose and l-galactose metabolism, and transcriptionally induced by these carbon sources; therefore, the physiological role remains unclear. Here, we report that AaFucM possesses mutarotation activity only toward l-fucose by saturation difference (SD) NMR experiments. Moreover, we determined the crystal structures of AaFucM in the apo form and in the l-fucose-bound form at resolutions of 2.21 and 1.75 A, respectively. The overall structural folding was clearly similar to the RhaM members, differed from the known l-fucose mutarotase (COG4154: FucU), strongly indicating their convergent evolution. The structure-based mutational analyses suggest that Tyr18 is important for catalytic action, and that Gln87 and Trp99 are involved in the l-fucose-specific recognition. Functional and structural characterization of a novel L-fucose mutarotase involved in non-phosphorylative pathway of L-fucose metabolism.,Watanabe Y, Watanabe S, Fukui Y, Nishiwaki H Biochem Biophys Res Commun. 2020 May 21. pii: S0006-291X(20)31015-9. doi:, 10.1016/j.bbrc.2020.05.094. PMID:32448506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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