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

doi:10.1107/S2053230X21008943

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 journal › Article › peer-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 language	English
Pages (from-to)	328-333
Number of pages	6
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	77
DOIs	https://doi.org/10.1107/S2053230X21008943
State	Published - 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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Cite this

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

abstract = "The 1.5 {\AA} 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.",

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AU - Miller, Mitchell D.

AU - Bhardwaj, Minakshi

AU - Thorson, Jon S.

AU - van Lanen, Steven G.

AU - Phillips, George N.

PY - 2021/10/1

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AB - 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.

KW - DynU16

KW - Dynemicin

KW - Helix-grip fold

KW - START/Bet v1 domain

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JO - Acta Crystallographica Section F:Structural Biology Communications

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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