2pc8 | pdb_00002pc8

E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A

spinqualitylabelsall models 2pc8, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pc8 is a 1 chain structure with sequence from monilia_stellatoidea Atcc 11006 monilia stellatoidea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC Related: 1eqp, 1eqc, 2pb1, 2pbo Gene: XOG1 (ATCC 11006 Monilia stellatoidea) Activity: Glucan 1,3-beta-glucosidase, with EC number 3.2.1.58 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EXG_CANAL] Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase. 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 Candida albicans exo-beta-1,3-glucanase (Exg; EC 3.2.1.58) is implicated in cell wall beta-d-glucan remodelling through its glucosyl hydrolase and/or transglucosylase activities. A pair of antiparallel phenylalanyl residues (F144 and F258) flank the entrance to the active site pocket. Various Exg mutants were studied using steady-state kinetics and crystallography aiming to understand the roles played by these residues in positioning the beta-1,3-d-glucan substrate. Mutations at the Phe-Phe entranceway demonstrated the requirement for double-sided CH/pi interactions at the +1 subsite, and the necessity for phenylalanine rather than tyrosine or tryptophan. The Tyr-Tyr double mutations introduced ordered water molecules into the entranceway. A third Phe residue (F229) nearby was evaluated as a possible +2 subsite. The inactive double mutant E292S/F229A complexed with laminaritriose has provided the first picture of substrate binding to Exg and demonstrated how the Phe-Phe arrangement acts as a clamp at the +1 subsite. The terminal sugar at the -1 site showed displacement from the position of a monosaccharide analogue with interchange of water molecules and sugar hydroxyls. An unexpected additional glucose binding site, well removed from the active site, was revealed. This site may enable Exg to associate with the branched glucan structure of the C. albicans cell wall. Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance.,Patrick WM, Nakatani Y, Cutfield SM, Sharpe ML, Ramsay RJ, Cutfield JF FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07869.x. PMID:20875088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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