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TitleAspartic acid residues in BBE-like enzymes from Morus alba promote a function shift from oxidative cyclization to dehydrogenation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 122, Page e2504346122-e2504346122, Year 2025
Publish dateMay 21, 2024 (structure data deposition date)
AuthorsGuo, N. / Gu, J. / Zhou, Q. / Liu, F. / Dong, H. / Ding, Q. / Wang, Q. / Wu, D. / Yang, J. / Fan, J. ...Guo, N. / Gu, J. / Zhou, Q. / Liu, F. / Dong, H. / Ding, Q. / Wang, Q. / Wu, D. / Yang, J. / Fan, J. / Gao, L. / Houk, K.N. / Lei, X.
External linksProc. Natl. Acad. Sci. USA / PubMed:40828030
MethodsX-ray diffraction
Resolution2.03 - 2.21 Å
Structure data

PDB-8zls:
Apo structure of BBE-like oxidative cyclase MaDS1
Method: X-RAY DIFFRACTION / Resolution: 2.21 Å

PDB-8zlt:
Co-crystal structure of MaDS1 with diene
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

PDB-1d8f:
CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A PIPERAZINE BASED INHIBITOR.

Source
  • morus alba (white mulberry)
KeywordsPLANT PROTEIN / BBE-like enzyme / Oxidative cyclase / FLAVOPROTEIN / Oxidase

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