4WLC
Structure of dextran glucosidase with glucose
Summary for 4WLC
| Entry DOI | 10.2210/pdb4wlc/pdb |
| Descriptor | Glucan 1,6-alpha-glucosidase, beta-D-glucopyranose, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | glycoside hydrolase, dextran glucosidase, intermediate, complex, hydrolase |
| Biological source | Streptococcus mutans UA159 |
| Total number of polymer chains | 1 |
| Total formula weight | 62549.42 |
| Authors | Kobayashi, M.,Kato, K.,Yao, M. (deposition date: 2014-10-07, release date: 2015-08-26, Last modification date: 2024-10-23) |
| Primary citation | Kobayashi, M.,Saburi, W.,Nakatsuka, D.,Hondoh, H.,Kato, K.,Okuyama, M.,Mori, H.,Kimura, A.,Yao, M. Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase Febs Lett., 589:484-489, 2015 Cited by PubMed Abstract: Streptococcus mutans dextran glucosidase (SmDG) belongs to glycoside hydrolase family 13, and catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form α-(1→6)-glucosidic linkage at the substrate non-reducing ends. Here, we report the 2.4Å resolution crystal structure of glucosyl-enzyme intermediate of SmDG. In the obtained structure, the Trp238 side-chain that constitutes the substrate-binding site turned away from the active pocket, concurrently with conformational changes of the nucleophile and the acid/base residues. Different conformations of Trp238 in each reaction stage indicated its flexibility. Considering the results of kinetic analyses, such flexibility may reflect a requirement for the reaction mechanism of SmDG. PubMed: 25595454DOI: 10.1016/j.febslet.2015.01.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.402 Å) |
Structure validation
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