4QNW
Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus
Summary for 4QNW
| Entry DOI | 10.2210/pdb4qnw/pdb |
| Descriptor | Chanoclavine-I aldehyde reductase, FLAVIN MONONUCLEOTIDE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | ergot alkaloid, old yellow enzyme, alpha/beta barrel, reductase, oxidoreductase |
| Biological source | Aspergillus fumigatus |
| Total number of polymer chains | 1 |
| Total formula weight | 44909.46 |
| Authors | Lamb, A.L. (deposition date: 2014-06-18, release date: 2014-10-22, Last modification date: 2023-09-20) |
| Primary citation | Chilton, A.S.,Ellis, A.L.,Lamb, A.L. Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis. Acta Crystallogr.,Sect.F, 70:1328-1332, 2014 Cited by PubMed Abstract: The Aspergillus fumigatus old yellow enzyme (OYE) EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways. The crystal structure of the FMN-loaded EasA was determined to 1.8 Å resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the α/β-unsaturated aldehyde. The C-terminal tail of one monomer packs into the active site of a monomer in the next asymmetric unit, which is most likely to be a crystallization artifact and not a mechanism of self-regulation. PubMed: 25286934DOI: 10.1107/S2053230X14018962 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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