Published 2013 | Version v1
Journal article Metadata-only

The binding mode of Ni-(L-His)2 in NikA revealed by X-ray crystallography

Creators

  • 1. Institut de Biologie Structurale Jean-Pierre Ebel, Metalloproteins Group, UMR 5075, CEA, DSV, CNRS, Universite Joseph Fourier-Grenoble 1, 41, rue Jules Horowitz 38027 Grenoble Cedex 1, (France)

Description

The ABC-type importer NikABCDE mediates nickel acquisition in Escherichia coli. The periplasmic nickel binding component NikA has a folding similar to that of the peptide transporter OppA and does not bind free nickel. Instead, we showed that the metal is tetra-coordinated by an organic tri-dentate molecule and His416. Conversely, it has been recently reported that NikA binds Ni-(L-His)2 and that addition of histidine increases the rate of nickel uptake in vivo. Here, we report the structure of NikA/Ni-(L-His)2 and show that histidine binding differs from peptide binding in OppA. The structure also confirms the central role of His416 in nickel binding. (authors)

Availability note (English)

Available from doi: http://dx.doi.org/10.1016/j.jinorgbio.2012.12.010

Additional details

Identifiers

DOI
10.1016/j.jinorgbio.2012.12.010;

Publishing Information

Journal Title
Journal of Inorganic Biochemistry
Journal Volume
121
Journal Page Range
p. 16-18
ISSN
0162-0134

INIS

Country of Publication
United States
Country of Input or Organization
France
INIS RN
47028734
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ESCHERICHIA COLI; HISTIDINE; IN VIVO; NICKEL; UPTAKE; X-RAY DIFFRACTION
Descriptors DEC
AMINO ACIDS; AZOLES; BACTERIA; CARBOXYLIC ACIDS; COHERENT SCATTERING; DIFFRACTION; ELEMENTS; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; IMIDAZOLES; METALS; MICROORGANISMS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; SCATTERING; TRANSITION ELEMENTS

Optional Information

Notes
22 refs.