7BYU

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

Summary for 7BYU

• Entry DOI: 10.2210/pdb7byu/pdb
• Descriptor: L-fucose mutarotase, 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: l-fucose, mutarotase, sugar binding protein
• Biological source: Acidovorax avenae subsp. avenae ATCC 19860
• Total number of polymer chains: 2
• Total formula weight: 28916.50

Authors

Watanabe, Y.,Fukui, Y.,Watanabe, S. (deposition date: 2020-04-24, release date: 2020-05-27, Last modification date: 2023-11-29)

Primary citation

Watanabe, Y.,Watanabe, S.,Fukui, Y.,Nishiwaki, H.
Functional and structural characterization of a novel L-fucose mutarotase involved in non-phosphorylative pathway of L-fucose metabolism.
Biochem.Biophys.Res.Commun., 528:21-27, 2020

PubMed Abstract: Mutarotases catalyze the α-β anomeric conversion of monosaccharide, and play a key role in utilizing sugar as enzymes involved in sugar metabolism have specificity for the α- or β-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 Å, 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.

PubMed: 32448506
DOI: 10.1016/j.bbrc.2020.05.094

Experimental method

X-RAY DIFFRACTION (2.206 Å)