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Article

Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility

1
Aix Marseille Univ, CNRS, BIP, Bioénergétique et Ingénierie des Protéines, IMM, Marseille, France
2
Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, 40127 Bologna, Italy
*
Authors to whom correspondence should be addressed.
Biomolecules 2020, 10(7), 1062; https://doi.org/10.3390/biom10071062
Received: 2 June 2020 / Revised: 25 June 2020 / Accepted: 10 July 2020 / Published: 16 July 2020
(This article belongs to the Special Issue The Amazing World of IDPs in Human Diseases)
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. View Full-Text
Keywords: intrinsically disordered proteins; EPR spectroscopy; isothermal titration calorimetry; protein-ligand interaction; site-directed spin labeling; protein structural dynamics intrinsically disordered proteins; EPR spectroscopy; isothermal titration calorimetry; protein-ligand interaction; site-directed spin labeling; protein structural dynamics
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MDPI and ACS Style

Pierro, A.; Etienne, E.; Gerbaud, G.; Guigliarelli, B.; Ciurli, S.; Belle, V.; Zambelli, B.; Mileo, E. Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility. Biomolecules 2020, 10, 1062. https://doi.org/10.3390/biom10071062

AMA Style

Pierro A, Etienne E, Gerbaud G, Guigliarelli B, Ciurli S, Belle V, Zambelli B, Mileo E. Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility. Biomolecules. 2020; 10(7):1062. https://doi.org/10.3390/biom10071062

Chicago/Turabian Style

Pierro, Annalisa, Emilien Etienne, Guillaume Gerbaud, Bruno Guigliarelli, Stefano Ciurli, Valérie Belle, Barbara Zambelli, and Elisabetta Mileo. 2020. "Nickel and GTP Modulate Helicobacter pylori UreG Structural Flexibility" Biomolecules 10, no. 7: 1062. https://doi.org/10.3390/biom10071062

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