2OXB
Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose
Summary for 2OXB
| Entry DOI | 10.2210/pdb2oxb/pdb |
| Related | 2AC1 |
| Related PRD ID | PRD_900003 |
| Descriptor | Beta-fructofuranosidase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Secreted, extracellular space, apoplast (Probable): Q43866 |
| Total number of polymer chains | 1 |
| Total formula weight | 62107.98 |
| Authors | Lammens, W.,Le Roy, K.,Van Laere, A.,Van den Ende, W.,Rabijns, A. (deposition date: 2007-02-20, release date: 2008-01-22, Last modification date: 2023-08-30) |
| Primary citation | Matrai, J.,Lammens, W.,Jonckheer, A.,Le Roy, K.,Rabijns, A.,Van den Ende, W.,De Maeyer, M. An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study. Proteins, 71:552-564, 2007 Cited by PubMed Abstract: In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme. PubMed: 17963237DOI: 10.1002/prot.21700 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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