5XXL
Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron
Summary for 5XXL
| Entry DOI | 10.2210/pdb5xxl/pdb |
| Related | 5XXM 5XXN 5XXO |
| Descriptor | Periplasmic beta-glucosidase, MAGNESIUM ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | glycoside hydrolase family 3, beta-glucosidase, hydrolase |
| Biological source | Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) |
| Total number of polymer chains | 2 |
| Total formula weight | 168386.03 |
| Authors | Nakajima, M.,Ishiguro, R.,Tanaka, N.,Abe, K.,Maeda, T.,Miyanaga, A.,Takahash, Y.,Sugimoto, N.,Nakai, H.,Taguchi, H. (deposition date: 2017-07-04, release date: 2017-12-13, Last modification date: 2023-11-22) |
| Primary citation | Ishiguro, R.,Tanaka, N.,Abe, K.,Nakajima, M.,Maeda, T.,Miyanaga, A.,Takahashi, Y.,Sugimoto, N.,Nakai, H.,Taguchi, H. Function and structure relationships of a beta-1,2-glucooligosaccharide-degrading beta-glucosidase. FEBS Lett., 591:3926-3936, 2017 Cited by PubMed Abstract: BT_3567 protein, a putative β-glucosidase from Bacteroides thetaiotaomicron, exhibits higher activity toward Sop (Sop , n: degree of polymerization of β-1,2-glucooligosaccharides) than toward Sop , unlike a known β-glucosidase from Listeria innocua which predominantly prefers Sop . In the complex structure determined by soaking of a D286N mutant crystal with Sop , a Sop moiety was observed at subsites -1 to +2. The glucose moiety at subsite +2 forms a hydrogen bond with Asn81, which is replaced with Gly in the L. innocua β-glucosidase. The K values of the N81G mutant for Sop are much higher than those of the wild-type, suggesting that Asn81 contributes to the binding to substrates longer than Sop . PubMed: 29131329DOI: 10.1002/1873-3468.12911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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