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

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 compatib...

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Detalles Bibliográficos
Autores principales: Alvarado, Sarah K., Miller, Mitchell D., Bhardwaj, Minakshi, Thorson, Jon S., Van Lanen, Steven G., Phillips, George N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8488855/
https://www.ncbi.nlm.nih.gov/pubmed/34605436
http://dx.doi.org/10.1107/S2053230X21008943
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author Alvarado, Sarah K.
Miller, Mitchell D.
Bhardwaj, Minakshi
Thorson, Jon S.
Van Lanen, Steven G.
Phillips, George N.
author_facet Alvarado, Sarah K.
Miller, Mitchell D.
Bhardwaj, Minakshi
Thorson, Jon S.
Van Lanen, Steven G.
Phillips, George N.
author_sort Alvarado, Sarah K.
collection PubMed
description 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.
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spelling pubmed-84888552021-10-18 Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis Alvarado, Sarah K. Miller, Mitchell D. Bhardwaj, Minakshi Thorson, Jon S. Van Lanen, Steven G. Phillips, George N. Acta Crystallogr F Struct Biol Commun Research Communications 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. International Union of Crystallography 2021-09-21 /pmc/articles/PMC8488855/ /pubmed/34605436 http://dx.doi.org/10.1107/S2053230X21008943 Text en © Sarah K. Alvarado et al. 2021 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Alvarado, Sarah K.
Miller, Mitchell D.
Bhardwaj, Minakshi
Thorson, Jon S.
Van Lanen, Steven G.
Phillips, George N.
Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title_full Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title_fullStr Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title_full_unstemmed Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title_short Structural characterization of DynU16, a START/Bet v1-like protein involved in dynemicin biosynthesis
title_sort structural characterization of dynu16, a start/bet v1-like protein involved in dynemicin biosynthesis
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8488855/
https://www.ncbi.nlm.nih.gov/pubmed/34605436
http://dx.doi.org/10.1107/S2053230X21008943
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