The Complex Energy Landscape of the Protein IscU

Biophysical Journal
Jameson R BotheJohn L Markley

Abstract

IscU, the scaffold protein for iron-sulfur (Fe-S) cluster biosynthesis in Escherichia coli, traverses a complex energy landscape during Fe-S cluster synthesis and transfer. Our previous studies showed that IscU populates two interconverting conformational states: one structured (S) and one largely disordered (D). Both states appear to be functionally important because proteins involved in the assembly or transfer of Fe-S clusters have been shown to interact preferentially with either the S or D state of IscU. To characterize the complex structure-energy landscape of IscU, we employed NMR spectroscopy, small-angle x-ray scattering (SAXS), and differential scanning calorimetry. Results obtained for IscU at pH 8.0 show that its S state is maximally populated at 25°C and that heating or cooling converts the protein toward the D state. Results from NMR and DSC indicate that both the heat- and cold-induced S→D transitions are cooperative and two-state. Low-resolution structural information from NMR and SAXS suggests that the structures of the cold-induced and heat-induced D states are similar. Both states exhibit similar (1)H-(15)N HSQC spectra and the same pattern of peptidyl-prolyl peptide bond configurations by NMR, and both appea...Continue Reading

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Citations

Feb 9, 2017·Biochemistry·Heike I RösnerBirthe B Kragelund
Aug 5, 2020·Proceedings of the National Academy of Sciences of the United States of America·Ignacio Díaz-FranulicRamon Latorre
Sep 12, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Kai Cai, John L Markley
Jun 16, 2021·Scientific Reports·Mana Mohan RabhaAnurup Gohain Barua
May 23, 2018·ACS Chemical Biology·Acacia F Dishman, Brian F Volkman

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Methods Mentioned

BETA
NMR
differential
x-ray scattering
gel filtration
X-Ray
circular dichroism

Software Mentioned

ScÅtter
NMRPipe
SHAKE
ATSAS
AMBER
MES

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