3ZSE
3D Structure of a thermophilic family GH11 xylanase from Thermobifida fusca
Summary for 3ZSE
| Entry DOI | 10.2210/pdb3zse/pdb |
| Descriptor | ENDO-1,4-BETA-XYLANASE, beta-D-xylopyranose-(1-4)-2-deoxy-2-fluoro-alpha-D-xylopyranose, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | hydrolase, glycoside hydrolase, plant cell wall |
| Biological source | THERMOBIFIDA FUSCA |
| Total number of polymer chains | 1 |
| Total formula weight | 22845.59 |
| Authors | Lammerts van Bueren, A.,Otani, S.,Friis, E.P.,S Wilson, K.,Davies, G.J. (deposition date: 2011-06-27, release date: 2012-02-08, Last modification date: 2024-10-23) |
| Primary citation | Lammerts Van Bueren, A.,Otani, S.,Friis, E.P.,Wilson, K.S.,Davies, G.J. Three-Dimensional Structure of a Thermophilic Family Gh11 Xylanase from Thermobifida Fusca. Acta Crystallogr.,Sect.F, 68:141-, 2012 Cited by PubMed Abstract: Thermostable enzymes employ various structural features dictated at the amino-acid sequence level that allow them to maintain their integrity at higher temperatures. Many hypotheses as to the nature of thermal stability have been proposed, including optimized core hydrophobicity and an increase in charged surface residues to enhance polar solvent interactions for solubility. Here, the three-dimensional structure of the family GH11 xylanase from the moderate thermophile Thermobifida fusca in its trapped covalent glycosyl-enzyme intermediate complex is presented. Interactions with the bound ligand show fewer direct hydrogen bonds from ligand to protein than observed in previous complexes from other species and imply that binding of the xylan substrate involves several water-mediated hydrogen bonds. PubMed: 22297985DOI: 10.1107/S1744309111049608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
Download full validation report
