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.

Funding

Funding for this research was provided by: National Institutes of Health, National Institute of General Medical Sciences (grant No. GM115261 to George N. Phillips Jr, Jon S. Thorson; studentship No. T32GM0082280 to Sarah K. Alvarado); National Institutes of Health, National Cancer Institute (grant No. CA217255 to George N. Phillips Jr, Jon S. Thorson, Steven G. Van Lanen); National Science Foundation, BioXFEL Science and Technology Center (grant No. 1231306 to George N. Phillips Jr). This work used research resources provided by the University of Kentucky Center of Biomedical Research Excellence (COBRE) in Pharmaceutical Research and Innovation (CPRI; NIH P20 GM130456), College of Pharmacy and the National Center for Advancing Translational Sciences (UL1TR000117 and UL1TR001998). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health or the National Science Foundation.

Funders	Funder number
Corporacion Nacional del Cobre
University of Kentucky Center for Biomedical Research Excellence
National Science Foundation (NSF)
National Institutes of Health (NIH)	P20 GM130456
Michigan State University-U.S. Department of Energy (MSU-DOE) Plant Research Laboratory
National Childhood Cancer Registry – National Cancer Institute	CA217255
National Institute of General Medical Sciences	T32GM0082280, GM115261, T32GM008280
Michigan Economic Development Corporation
National Center for Advancing Translational Sciences (NCATS)	UL1TR001998, UL1TR000117
Office of Science Programs
Argonne National Laboratory	DE-AC02-06CH11357
BioXFEL Science and Technology Center	1231306
Michigan Technology Tri-Corridor	085P1000817

Keywords

DynU16
Dynemicin
Helix-grip fold
START/Bet v1 domain

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

Access to Document

10.1107/S2053230X21008943

Cite this

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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 - Thorson, Jon S.

AU - van Lanen, Steven G.

AU - Phillips, George N.

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

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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