4BF7
Emericilla nidulans endo-beta-1,4-galactanase
Summary for 4BF7
| Entry DOI | 10.2210/pdb4bf7/pdb |
| Descriptor | ARABINOGALACTAN ENDO-1,4-BETA-GALACTOSIDASE A, ZINC ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Cellular location | Secreted (By similarity): Q5B153 |
| Total number of polymer chains | 1 |
| Total formula weight | 40749.64 |
| Authors | Otten, H.,Michalak, M.,Larsen, S.,Mikkelsen, J.D. (deposition date: 2013-03-15, release date: 2013-08-07, Last modification date: 2024-11-13) |
| Primary citation | Otten, H.,Michalak, M.,Mikkelsen, J.D.,Larsen, S. The Binding of Zinc Ions to Emericella Nidulans Endo-[Beta]-1,4-Galactanase is Essential for Crystal Formation Acta Crystallogr.,Sect.F, 69:850-, 2013 Cited by PubMed Abstract: A novel Emericella nidulans endo-β-1,4-galactanase (EnGAL) demonstrates a strong capacity to generate high levels of very potent prebiotic oligosaccharides from potato pulp, a by-product of the agricultural potato-starch industry. EnGAL belongs to glycoside hydrolase family 53 and shows high (72.5%) sequence identity to an endo-β-1,4-galactanase from Aspergillus aculeatus. Diffraction data extending to 2.0 Å resolution were collected from a crystal of EnGAL grown from conditions containing 0.2 M zinc acetate. The crystal structure showed a high similarity between EnGAL and other endo-β-1,4-galactanases belonging to GH53. It also revealed 15 zinc ions bound to the protein, one of which is located in the active site, where it is coordinated by residues Glu136 and Glu246 which comprise the catalytic machinery. The majority of the zinc ions are located on the surface of the enzyme, in some cases with side chains from two different molecules as ligands, thus explaining why the presence of zinc ions was essential for crystallization. PubMed: 23908026DOI: 10.1107/S1744309113019714 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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