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TitleStructure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 1538, Year 2023
Publish dateMar 20, 2023
AuthorsShivesh Kumar / Yan Wang / Ye Zhou / Lucas Dillard / Fay-Wei Li / Carly A Sciandra / Ning Sui / Rodolfo Zentella / Emily Zahn / Jeffrey Shabanowitz / Donald F Hunt / Mario J Borgnia / Alberto Bartesaghi / Tai-Ping Sun / Pei Zhou /
PubMed AbstractSPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is ...SPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is distinct from ER-localized POFUTs and contains N-terminal tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain resembling the O-linked-N-acetylglucosamine (GlcNAc) transferases (OGTs). However, the structural feature that determines the distinct enzymatic selectivity of SPY remains unknown. Here we report the cryo-electron microscopy (cryo-EM) structure of SPY and its complex with GDP-fucose, revealing distinct active-site features enabling GDP-fucose instead of UDP-GlcNAc binding. SPY forms an antiparallel dimer instead of the X-shaped dimer in human OGT, and its catalytic domain interconverts among multiple conformations. Analysis of mass spectrometry, co-IP, fucosylation activity, and cryo-EM data further demonstrates that the N-terminal disordered peptide in SPY contains trans auto-fucosylation sites and inhibits the POFUT activity, whereas TPRs 1-5 dynamically regulate SPY activity by interfering with protein substrate binding.
External linksNat Commun / PubMed:36941311 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.2 Å
Structure data

EMDB-27701: Focused map (monomer A) for Arabidopsis SPY in complex with GDP-fucose
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-27702: Focused map (monomer B) for Arabidopsis SPY in complex with GDP-fucose
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • Arabidopsis thaliana (thale cress)

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