4lx4 | pdb_00004lx4

Crystal Structure Determination of Pseudomonas stutzeri endoglucanase Cel5A using a Twinned Data Set

spinqualitylabelsall models 4lx4, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lx4 is a 4 chain structure with sequence from Pseudomonas stutzeri A1501. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4VME5_PSEU5 Publication Abstract from PubMed The discovery of new glycoside hydrolases that can be utilized in the chemoenzymatic synthesis of carbohydrates has emerged as a promising approach for various biotechnological processes. In this study, recombinant Ps_Cel5A from Pseudomonas stutzeri A1501, a novel member of the GH5_5 subfamily, was expressed, purified and crystallized. Preliminary experiments confirmed the ability of Ps_Cel5A to catalyze transglycosylation with cellotriose as a substrate. The crystal structure revealed several structural determinants in and around the positive subsites, providing a molecular basis for a better understanding of the mechanisms that promote and favour synthesis rather than hydrolysis. In the positive subsites, two nonconserved positively charged residues (Arg178 and Lys216) were found to interact with cellobiose. This adaptation has also been reported for transglycosylating beta-mannanases of the GH5_7 subfamily. Crystal structure determination of Pseudomonas stutzeri A1501 endoglucanase Cel5A: the search for a molecular basis for glycosynthesis in GH5_5 enzymes.,Dutoit R, Delsaute M, Collet L, Vander Wauven C, Van Elder D, Berlemont R, Richel A, Galleni M, Bauvois C Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):605-615. doi:, 10.1107/S2059798319007113. Epub 2019 Jun 6. PMID:31205022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase 3D structures

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