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An XAS investigation of the nickel site structure in the transcriptional regulator InrS

Carr, Carolyn E.; Foster, Andrew W.; Maroney, Michael J.

An XAS investigation of the nickel site structure in the transcriptional regulator InrS Thumbnail


Authors

Carolyn E. Carr

Andrew W. Foster

Michael J. Maroney



Abstract

InrS (Internal nickel-responsive Sensor) is a transcriptional repressor of the nickel exporter NrsD and de-represses expression of the exporter upon binding Ni(II) ions. Although a crystal structure of apo-InrS has been reported, no structure of the protein with metal ions bound is available. Herein we report the results of metal site structural investigations of Ni(II) and Cu(II) complexes of InrS using X-ray absorption spectroscopy (XAS) that are complementary to data available from the apo-InrS crystal structure, and are consistent with a planar four-coordinate [Ni(His)2(Cys)2] structure, where the ligands are derived from the side chains of His21, Cys53, His78, and Cys82. Coordination of Cu(II) to InrS forms a nearly identical planar four-coordinate complex that is consistent with a simple replacement of the Ni(II) center by Cu(II).

Citation

Carr, C. E., Foster, A. W., & Maroney, M. J. (2017). An XAS investigation of the nickel site structure in the transcriptional regulator InrS. Journal of Inorganic Biochemistry, 177, 352-358. https://doi.org/10.1016/j.jinorgbio.2017.08.003

Journal Article Type Article
Acceptance Date Aug 5, 2017
Online Publication Date Aug 10, 2017
Publication Date Dec 1, 2017
Deposit Date Oct 5, 2017
Publicly Available Date Mar 29, 2024
Journal Journal of Inorganic Biochemistry
Print ISSN 0162-0134
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 177
Pages 352-358
DOI https://doi.org/10.1016/j.jinorgbio.2017.08.003

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