8AKP
Crystal structure of the catalytic domain of G7048 from Penicillium sumatraense
Summary for 8AKP
Entry DOI | 10.2210/pdb8akp/pdb |
Descriptor | catalytic domain of G7048, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
Functional Keywords | cell wall-degrading enzymes, 1, 3-beta-trans-glucanase, tim-barrel, hydrolase |
Biological source | Penicillium sumatraense |
Total number of polymer chains | 1 |
Total formula weight | 32440.28 |
Authors | Troilo, F.,Scafati, V.,Giovannoni, M.,Mattei, B.,Benedetti, M.,Angelucci, F.,Di Matteo, A. (deposition date: 2022-07-30, release date: 2022-12-28, Last modification date: 2024-10-23) |
Primary citation | Scafati, V.,Troilo, F.,Ponziani, S.,Giovannoni, M.,Scortica, A.,Pontiggia, D.,Angelucci, F.,Di Matteo, A.,Mattei, B.,Benedetti, M. Characterization of two 1,3-beta-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-beta-glucan metabolism of fungal saprotrophs. Biotechnol Biofuels Bioprod, 15:138-138, 2022 Cited by PubMed Abstract: 1,3-β-glucan is a polysaccharide widely distributed in the cell wall of several phylogenetically distant organisms, such as bacteria, fungi, plants and microalgae. The presence of highly active 1,3-β-glucanases in fungi evokes the biological question on how these organisms can efficiently metabolize exogenous sources of 1,3-β-glucan without incurring in autolysis. PubMed: 36510318DOI: 10.1186/s13068-022-02233-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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