Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.

FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction prod...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Julien Robert-Paganin, Sylvie Nonin-Lecomte, Stéphane Réty
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/03b56585a7c84cc4a021c0a6d6f10680
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:03b56585a7c84cc4a021c0a6d6f10680
record_format	dspace
spelling	oai:doaj.org-article:03b56585a7c84cc4a021c0a6d6f106802021-11-18T08:04:10ZCrystal structure of an EAL domain in complex with reaction product 5'-pGpG.1932-620310.1371/journal.pone.0052424https://doaj.org/article/03b56585a7c84cc4a021c0a6d6f106802012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23285035/?tool=EBIhttps://doaj.org/toc/1932-6203FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains.Julien Robert-PaganinSylvie Nonin-LecomteStéphane RétyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 12, p e52424 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Julien Robert-Paganin Sylvie Nonin-Lecomte Stéphane Réty Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
description	FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains.
format	article
author	Julien Robert-Paganin Sylvie Nonin-Lecomte Stéphane Réty
author_facet	Julien Robert-Paganin Sylvie Nonin-Lecomte Stéphane Réty
author_sort	Julien Robert-Paganin
title	Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
title_short	Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
title_full	Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
title_fullStr	Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
title_full_unstemmed	Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
title_sort	crystal structure of an eal domain in complex with reaction product 5'-pgpg.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/03b56585a7c84cc4a021c0a6d6f10680
work_keys_str_mv	AT julienrobertpaganin crystalstructureofanealdomainincomplexwithreactionproduct5pgpg AT sylvienoninlecomte crystalstructureofanealdomainincomplexwithreactionproduct5pgpg AT stephanerety crystalstructureofanealdomainincomplexwithreactionproduct5pgpg
_version_	1718422269120741376

Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.

Ejemplares similares