About: Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility
Creator	Belle, Valérie Ciurli, Stefano Etienne, Emilien Gerbaud, Guillaume Guigliarelli, Bruno Mileo, Elisabetta Pierro, Annalisa Zambelli, Barbara
source	PMC
abstract	UreG is a P-loop GTP hydrolase involved in the maturation of nickel-containing urease, an essential enzyme found in plants, fungi, bacteria, and archaea. This protein couples the hydrolysis of GTP to the delivery of Ni(II) into the active site of apo-urease, interacting with other urease chaperones in a multi-protein complex necessary for enzyme activation. Whereas the conformation of Helicobacter pylori (Hp) UreG was solved by crystallography when it is in complex with two other chaperones, in solution the protein was found in a disordered and flexible form, defining it as an intrinsically disordered enzyme and indicating that the well-folded structure found in the crystal state does not fully reflect the behavior of the protein in solution. Here, isothermal titration calorimetry and site-directed spin labeling coupled to electron paramagnetic spectroscopy were successfully combined to investigate HpUreG structural dynamics in solution and the effect of Ni(II) and GTP on protein mobility. The results demonstrate that, although the protein maintains a flexible behavior in the metal and nucleotide bound forms, concomitant addition of Ni(II) and GTP exerts a structural change through the crosstalk of different protein regions.
has issue date	2020-07-16(xsd:dateTime)
bibo:doi	10.3390/biom10071062
bibo:pmid	32708696
has license	cc-by
sha1sum (hex)	63d3b1b4158bc4c7923ea41d3813e3225e3e1097
schema:url	https://doi.org/10.3390/biom10071062
resource representing a document's title	Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility
has PubMed Central identifier	PMC7408563
has PubMed identifier	32708696
schema:publication	Biomolecules
resource representing a document's body	covid:63d3b1b4158bc4c7923ea41d3813e3225e3e1097#body_text
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