Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation

Pupylation is a bacterial post-translational protein modification, where the small ubiquitin-like protein Pup is covalently attached to lysine side chains of target proteins, which is a reversible process and depupylation is catalysed by the depupylase enzyme, Dop. Here, the authors present crystal...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Hengjun Cui, Andreas U. Müller, Marc Leibundgut, Jiawen Tian, Nenad Ban, Eilika Weber-Ban
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ee97e01ec2844a91ae1c01221884fb2b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ee97e01ec2844a91ae1c01221884fb2b
record_format	dspace
spelling	oai:doaj.org-article:ee97e01ec2844a91ae1c01221884fb2b2021-11-21T12:35:00ZStructures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation10.1038/s41467-021-26848-x2041-1723https://doaj.org/article/ee97e01ec2844a91ae1c01221884fb2b2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26848-xhttps://doaj.org/toc/2041-1723Pupylation is a bacterial post-translational protein modification, where the small ubiquitin-like protein Pup is covalently attached to lysine side chains of target proteins, which is a reversible process and depupylation is catalysed by the depupylase enzyme, Dop. Here, the authors present crystal structures of Dop in different functional states, which together with biochemical experiments provide insights into the catalytic mechanism of this enzyme.Hengjun CuiAndreas U. MüllerMarc LeibundgutJiawen TianNenad BanEilika Weber-BanNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hengjun Cui Andreas U. Müller Marc Leibundgut Jiawen Tian Nenad Ban Eilika Weber-Ban Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
description	Pupylation is a bacterial post-translational protein modification, where the small ubiquitin-like protein Pup is covalently attached to lysine side chains of target proteins, which is a reversible process and depupylation is catalysed by the depupylase enzyme, Dop. Here, the authors present crystal structures of Dop in different functional states, which together with biochemical experiments provide insights into the catalytic mechanism of this enzyme.
format	article
author	Hengjun Cui Andreas U. Müller Marc Leibundgut Jiawen Tian Nenad Ban Eilika Weber-Ban
author_facet	Hengjun Cui Andreas U. Müller Marc Leibundgut Jiawen Tian Nenad Ban Eilika Weber-Ban
author_sort	Hengjun Cui
title	Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
title_short	Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
title_full	Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
title_fullStr	Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
title_full_unstemmed	Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation
title_sort	structures of prokaryotic ubiquitin-like protein pup in complex with depupylase dop reveal the mechanism of catalytic phosphate formation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ee97e01ec2844a91ae1c01221884fb2b
work_keys_str_mv	AT hengjuncui structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation AT andreasumuller structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation AT marcleibundgut structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation AT jiawentian structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation AT nenadban structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation AT eilikaweberban structuresofprokaryoticubiquitinlikeproteinpupincomplexwithdepupylasedoprevealthemechanismofcatalyticphosphateformation
_version_	1718418921333194752

Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation

Ejemplares similares