7NDE
Trichoderma parareesei PL7A beta-glucuronan lyase
Summary for 7NDE
Entry DOI | 10.2210/pdb7nde/pdb |
Descriptor | Glucuronan lyase, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | glucuronan lyase, b-jelly roll, lyase |
Biological source | Trichoderma parareesei |
Total number of polymer chains | 1 |
Total formula weight | 25997.53 |
Authors | Fredslund, F.,Welner, D.H.,Wilkens, C. (deposition date: 2021-02-01, release date: 2022-03-02, Last modification date: 2024-10-16) |
Primary citation | Vuillemin, M.,Pilgaard, B.,Kiehn, E.,Fredslund, F.,Welner, D.H.,Meyer, A.S.,Aachmann, F.L.,Wilkens, C. Glucuronan lyases from family PL7 use a Tyr/Tyr syn beta-elimination catalytic mechanism for glucuronan breakdown. Chem.Commun.(Camb.), 60:440-443, 2024 Cited by PubMed Abstract: TpPL7A and TpPL7B, members of CAZy family PL7, act as β-glucuronan lyases. TpPL7A diverges by lacking the catalytic histidine, identified as the Brønsted base in PL7 alginate lyases. Our research, including TpPL7A's crystal structure, and mutagenesis studies, reveals a shared -β-elimination mechanism with a single tyrosine serving as both base and acid catalyst. This mechanism may extend to subfamily PL7_4 glucuronan lyases. PubMed: 38087900DOI: 10.1039/d3cc04256a PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
