2pwh | pdb_00002pwh

Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45

spinqualitylabelsall models 2pwh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pwh is a 2 chain structure with sequence from "pseudomonas_mesoacidophila"_kintaka_et_al._1981 "pseudomonas mesoacidophila" kintaka et al. 1981. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Related: 1zja, 1zjb, 2pwd, 2pwe, 2pwf, 2pwg Gene: mutB ("Pseudomonas mesoacidophila" Kintaka et al. 1981) Activity: Methylaspartate mutase, with EC number 5.4.99.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Various diseases related to the overconsumption of sugar make a growing need for sugar substitutes. Because sucrose is an inexpensive and readily available d-glucose donor, the industrial potential for enzymatic synthesis of the sucrose isomers trehalulose and/or isomaltulose from sucrose is large. The product specificity of sucrose isomerases that catalyze this reaction depends essentially on the possibility for tautomerization of sucrose, which is required for trehalulose formation. For optimal use of the enzyme, targeting controlled synthesis of these functional isomers, it is necessary to minimize the side reactions. This requires an extensive analysis of substrate binding modes and of the specificity-determining sites in the structure. The 1.6-2.2-A resolution three-dimensional structures of native and mutant complexes of a trehalulose synthase from Pseudomonas mesoacidophila MX-45 mimic successive states of the enzyme reaction. Combined with mutagenesis studies they give for the first time thorough insights into substrate recognition and processing and reaction specificities of these enzymes. Among the important outcomes of this study is the revelation of an aromatic clamp defined by Phe(256) and Phe(280) playing an essential role in substrate recognition and in controlling the reaction specificity, which is further supported by mutagenesis studies. Furthermore, this study highlights essential residues for binding the glucosyl and fructosyl moieties. The introduction of subtle changes informed by comparative three-dimensional structural data observed within our study can lead to fundamental modifications in the mode of action of sucrose isomerases and hence provide a template for industrial catalysts. Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.,Ravaud S, Robert X, Watzlawick H, Haser R, Mattes R, Aghajari N J Biol Chem. 2007 Sep 21;282(38):28126-36. Epub 2007 Jun 27. PMID:17597061 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trehalulose synthase

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