2ZZJ
Crystal structure of endo-beta-1,4-glucuronan lyase from fungus Trichoderma reesei
Summary for 2ZZJ
| Entry DOI | 10.2210/pdb2zzj/pdb |
| Descriptor | Glucuronan lyase A, CALCIUM ION, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | beta-jelly roll, lyase |
| Biological source | Trichoderma reesei (Hypocrea jecorina) |
| Total number of polymer chains | 1 |
| Total formula weight | 27569.02 |
| Authors | Konno, N.,Ishida, T.,Fushinobu, S.,Igarashi, K.,Habu, N.,Samejima, M.,Isogai, A. (deposition date: 2009-02-16, release date: 2009-05-05, Last modification date: 2024-11-13) |
| Primary citation | Konno, N.,Ishida, T.,Igarashi, K.,Fushinobu, S.,Habu, N.,Samejima, M.,Isogai, A. Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei. Febs Lett., 583:1323-1326, 2009 Cited by PubMed Abstract: The crystal structure of endo-beta-(1-->4)-glucuronan lyase from Trichoderma reesei (TrGL) has been determined at 1.8A resolution as the first three-dimensional structure of polysaccharide lyase (PL) family 20. TrGL has a typical beta-jelly roll fold, which is similar to glycoside hydrolase family 16 and PL7 enzymes. A calcium ion is bound to the site far from the cleft and appears to contribute to the stability. There are several completely conserved residues in the cleft. Possible catalytic residues are predicted based on structural comparison with PL7 alginate lyase A1-II'. PubMed: 19306878DOI: 10.1016/j.febslet.2009.03.034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report






