4LX4
Crystal Structure Determination of Pseudomonas stutzeri endoglucanase Cel5A using a Twinned Data Set
Summary for 4LX4
| Entry DOI | 10.2210/pdb4lx4/pdb |
| Descriptor | Endoglucanase(Endo-1,4-beta-glucanase)protein, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| Functional Keywords | glycosyl hydrolase family 5, cellulase, tim barrel, beta-1, 4-endoglucanase, hydrolase |
| Biological source | Pseudomonas stutzeri |
| Total number of polymer chains | 4 |
| Total formula weight | 149355.98 |
| Authors | Dutoit, R.,Delsaute, M.,Berlemont, R.,Van Elder, D.,Galleni, M.,Bauvois, C. (deposition date: 2013-07-29, release date: 2014-07-30, Last modification date: 2024-10-09) |
| Primary citation | Dutoit, R.,Delsaute, M.,Collet, L.,Vander Wauven, C.,Van Elder, D.,Berlemont, R.,Richel, A.,Galleni, M.,Bauvois, C. Crystal structure determination of Pseudomonas stutzeri A1501 endoglucanase Cel5A: the search for a molecular basis for glycosynthesis in GH5_5 enzymes. Acta Crystallogr D Struct Biol, 75:605-615, 2019 Cited by PubMed Abstract: 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 β-mannanases of the GH5_7 subfamily. PubMed: 31205022DOI: 10.1107/S2059798319007113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.556 Å) |
Structure validation
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