3kll | pdb_00003kll

Crystal structure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180-maltose complex

spinqualitylabelsall models 3kll, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kll is a 1 chain structure with sequence from Limosilactobacillus reuteri. The June 2011 RCSB PDB Molecule of the Month feature on Glucansucrase by David Goodsell is 10.2210/rcsb_pdb/mom_2011_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CA, GLC, GOL, MSE, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SBN3_LIMRT Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris.[ARBA:ARBA00003243] Publication Abstract from PubMed 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 alpha-glucan polymer. Among others, plaque-forming oral bacteria secrete these enzymes to produce alpha-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 alpha-amylase-like (beta/alpha)(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. Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes.,Vujicic-Zagar A, Pijning T, Kralj S, Lopez CA, Eeuwema W, Dijkhuizen L, Dijkstra BW Proc Natl Acad Sci U S A. 2010 Nov 30. PMID:21118988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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