6GSZ
Crystal structure of native alfa-L-rhamnosidase from Aspergillus terreus
Summary for 6GSZ
| Entry DOI | 10.2210/pdb6gsz/pdb |
| Descriptor | Alpha-L-rhamnosidase, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (18 entities in total) |
| Functional Keywords | hydrolase, glycosyl hydrolase, carbohydrate biotechnology, sulfur sad |
| Biological source | Aspergillus terreus |
| Total number of polymer chains | 1 |
| Total formula weight | 105552.74 |
| Authors | Pachl, P.,Rezacova, P.,Skerlova, J. (deposition date: 2018-06-15, release date: 2018-11-14, Last modification date: 2024-11-20) |
| Primary citation | Pachl, P.,Skerlova, J.,Simcikova, D.,Kotik, M.,Krenkova, A.,Mader, P.,Brynda, J.,Kapesova, J.,Kren, V.,Otwinowski, Z.,Rezacova, P. Crystal structure of native alpha-L-rhamnosidase from Aspergillus terreus. Acta Crystallogr D Struct Biol, 74:1078-1084, 2018 Cited by PubMed Abstract: α-L-Rhamnosidases cleave terminal nonreducing α-L-rhamnosyl residues from many natural rhamnoglycosides. This makes them catalysts of interest for various biotechnological applications. The X-ray structure of the GH78 family α-L-rhamnosidase from Aspergillus terreus has been determined at 1.38 Å resolution using the sulfur single-wavelength anomalous dispersion phasing method. The protein was isolated from its natural source in the native glycosylated form, and the active site contained a glucose molecule, probably from the growth medium. In addition to its catalytic domain, the α-L-rhamnosidase from A. terreus contains four accessory domains of unknown function. The structural data suggest that two of these accessory domains, E and F, might play a role in stabilizing the aglycon portion of the bound substrate. PubMed: 30387766DOI: 10.1107/S2059798318013049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.38 Å) |
Structure validation
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