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Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex

The enzyme ForT catalyzes C–C bond formation between 5′-phosphoribosyl-1′-pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3,5-dicarboxylate to make a key intermediate in the biosynthesis of formycin A 5′-phosphate by Streptomyces kaniharaensis. We report the 2.5 Å resolution structure of the ForT/PRPP...

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Detalles Bibliográficos
Autores principales: Gao, Sisi, Radadiya, Ashish, Li, Wenbo, Liu, Huanting, Zhu, Wen, de Crécy-Lagard, Valérie, Richards, Nigel G. J., Naismith, James H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8183095/
https://www.ncbi.nlm.nih.gov/pubmed/32515440
http://dx.doi.org/10.1039/d0cc02834g
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author Gao, Sisi
Radadiya, Ashish
Li, Wenbo
Liu, Huanting
Zhu, Wen
de Crécy-Lagard, Valérie
Richards, Nigel G. J.
Naismith, James H.
author_facet Gao, Sisi
Radadiya, Ashish
Li, Wenbo
Liu, Huanting
Zhu, Wen
de Crécy-Lagard, Valérie
Richards, Nigel G. J.
Naismith, James H.
author_sort Gao, Sisi
collection PubMed
description The enzyme ForT catalyzes C–C bond formation between 5′-phosphoribosyl-1′-pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3,5-dicarboxylate to make a key intermediate in the biosynthesis of formycin A 5′-phosphate by Streptomyces kaniharaensis. We report the 2.5 Å resolution structure of the ForT/PRPP complex and locate active site residues critical for PRPP recognition and catalysis.
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spelling pubmed-81830952021-06-07 Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex Gao, Sisi Radadiya, Ashish Li, Wenbo Liu, Huanting Zhu, Wen de Crécy-Lagard, Valérie Richards, Nigel G. J. Naismith, James H. Chem Commun (Camb) Chemistry The enzyme ForT catalyzes C–C bond formation between 5′-phosphoribosyl-1′-pyrophosphate (PRPP) and 4-amino-1H-pyrazole-3,5-dicarboxylate to make a key intermediate in the biosynthesis of formycin A 5′-phosphate by Streptomyces kaniharaensis. We report the 2.5 Å resolution structure of the ForT/PRPP complex and locate active site residues critical for PRPP recognition and catalysis. The Royal Society of Chemistry 2020-06-09 /pmc/articles/PMC8183095/ /pubmed/32515440 http://dx.doi.org/10.1039/d0cc02834g Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Gao, Sisi
Radadiya, Ashish
Li, Wenbo
Liu, Huanting
Zhu, Wen
de Crécy-Lagard, Valérie
Richards, Nigel G. J.
Naismith, James H.
Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title_full Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title_fullStr Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title_full_unstemmed Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title_short Uncovering the chemistry of C–C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex
title_sort uncovering the chemistry of c–c bond formation in c-nucleoside biosynthesis: crystal structure of a c-glycoside synthase/prpp complex
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8183095/
https://www.ncbi.nlm.nih.gov/pubmed/32515440
http://dx.doi.org/10.1039/d0cc02834g
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