Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis

Sarah K. Alvarado, Mitchell D. Miller, Minakshi Bhardwaj, Jon S. Thorson, Steven G. van Lanen, George N. Phillips

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The 1.5 Å resolution crystal structure of DynU16, a protein identified in the dynemicin-biosynthetic gene cluster, is reported. The structure adopts a di-domain helix-grip fold with a uniquely positioned open cavity connecting the domains. The elongated dimensions of the cavity appear to be compatible with the geometry of a linear polyene, suggesting the involvement of DynU16 in the upstream steps of dynemicin biosynthesis.

Original languageEnglish
Pages (from-to)328-333
Number of pages6
JournalActa Crystallographica Section F:Structural Biology Communications
Volume77
DOIs
StatePublished - Oct 1 2021

Bibliographical note

Publisher Copyright:
© 2021 International Union of Crystallography. All rights reserved.

Keywords

  • DynU16
  • Dynemicin
  • Helix-grip fold
  • START/Bet v1 domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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