期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 70, 期 -, 页码 1328-1332出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14018962
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资金
- Department of Energy, Office of Biological and Environmental Research
- National Institutes of Health, National Center for Research Resources, Biomedical Technology Program and the National Institute of General Medical Sciences
- National Institute for Allergy and Infectious Disease (ALL) [K02 AI093675]
- Kansas-IDeA Network for Biomedical Excellence Undergraduate Scholarship (ALE) from the National Center for Research Resources all from the National Institutes of Health [P20 RR016475]
- Kansas-IDeA Network for Biomedical Excellence Undergraduate Scholarship (ALE) from the National Institute of General Medical Sciences, all from the National Institutes of Health [P20GM103418]
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 angstrom resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the alpha/beta-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.
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