7XSG

Crystal structure of ClAgl29B

Summary for 7XSG

• Entry DOI: 10.2210/pdb7xsg/pdb
• Related: 7XSF
• Descriptor: Alpha-L-fucosidase, SODIUM ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: glycoside hydrolase, hydrolase
• Biological source: Cecembia lonarensis LW9
• Total number of polymer chains: 2
• Total formula weight: 135016.97

Authors

Shishiuchi, R.,Kang, H.,Tagami, T.,Okuyama, M. (deposition date: 2022-05-14, release date: 2023-01-18, Last modification date: 2024-04-03)

Primary citation

Shishiuchi, R.,Kang, H.,Tagami, T.,Ueda, Y.,Lang, W.,Kimura, A.,Okuyama, M.
Discovery of alpha-l-Glucosidase Raises the Possibility of alpha-l-Glucosides in Nature.
Acs Omega, 7:47411-47423, 2022

PubMed Abstract: Glucose, a common monosaccharide in nature, is dominated by the d-enantiomer. Meanwhile, the discovery of l-glucose-utilizing bacteria and the elucidation of their metabolic pathways 10 years ago suggests that l-glucose exists naturally. Most carbohydrates exist as glycosides rather than monosaccharides; therefore, we expected that nature also contains l-glucosides. Sequence analysis within glycoside hydrolase family 29 led us to identify two α-l-glucosidases, ClAgl29A and ClAgl29B, derived from LW9. ClAgl29A and ClAgl29B exhibited higher , , and / values for -nitrophenyl α-l-glucoside than that for -nitrophenyl α-l-fucoside. Structural analysis of ClAgl29B in complex with l-glucose showed that these enzymes have an active-site pocket that preferentially binds α-l-glucoside, but excludes α-l-fucoside. These results suggest that ClAgl29A and ClAgl29B evolved to hydrolyze α-l-glucoside, implying the existence of α-l-glucoside in nature. Furthermore, α-l-glucosidic linkages (α-l-Glc-(1 → 3)-l-Glc, α-l-Glc-(1 → 2)-l-Glc, and α-l-Glc-(1 → 6)-l-Glc) were synthesized by the transglucosylation activity of ClAgl29A and ClAgl29B. We believe that this study will lead to new research on α-l-glucosides, including determining the physiological effects on humans, and the discovery of novel α-l-glucoside-related enzymes.

PubMed: 36570207
DOI: 10.1021/acsomega.2c06991

Experimental method

X-RAY DIFFRACTION (1.609 Å)