3KLL
Crystal structure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180-maltose complex
Summary for 3KLL
| Entry DOI | 10.2210/pdb3kll/pdb |
| Related | 3HQ3 3HZ3 3KLK |
| Related PRD ID | PRD_900001 |
| Descriptor | Glucansucrase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | glucansucrase-maltose complex, multidomain protein, glycosyltransferase, transferase |
| Biological source | Lactobacillus reuteri |
| Total number of polymer chains | 1 |
| Total formula weight | 119544.98 |
| Authors | Vujicic-Zagar, A.,Pijning, T.,Kralj, S.,Eeuwema, W.,Dijkhuizen, L.,Dijkstra, B.W. (deposition date: 2009-11-08, release date: 2010-11-03, Last modification date: 2024-11-06) |
| Primary citation | Vujicic-Zagar, A.,Pijning, T.,Kralj, S.,Lopez, C.A.,Eeuwema, W.,Dijkhuizen, L.,Dijkstra, B.W. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes Proc.Natl.Acad.Sci.USA, 107:21406-21411, 2010 Cited by PubMed Abstract: Glucansucrases are large enzymes belonging to glycoside hydrolase family 70, which catalyze the cleavage of sucrose into fructose and glucose, with the concomitant transfer of the glucose residue to a growing α-glucan polymer. Among others, plaque-forming oral bacteria secrete these enzymes to produce α-glucans, which facilitate the adhesion of the bacteria to the tooth enamel. We determined the crystal structure of a fully active, 1,031-residue fragment encompassing the catalytic and C-terminal domains of GTF180 from Lactobacillus reuteri 180, both in the native state, and in complexes with sucrose and maltose. These structures show that the enzyme has an α-amylase-like (β/α)(8)-barrel catalytic domain that is circularly permuted compared to the catalytic domains of members of glycoside hydrolase families 13 and 77, which belong to the same GH-H superfamily. In contrast to previous suggestions, the enzyme has only one active site and one nucleophilic residue. Surprisingly, in GTF180 the peptide chain follows a "U"-path, such that four of the five domains are made up from discontiguous N- and C-terminal stretches of the peptide chain. Finally, the structures give insight into the factors that determine the different linkage types in the polymeric product. PubMed: 21118988DOI: 10.1073/pnas.1007531107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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