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Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS

Cite this: Biochemistry 2019, 58, 6, 687–696
Publication Date (Web):December 20, 2018
https://doi.org/10.1021/acs.biochem.8b01122
Copyright © 2018 American Chemical Society

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    Abstract

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    SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe–S cluster assembly pathway. In Escherichia coli, this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically, this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five X-ray crystal structures of SufS including a new structure of SufS containing an inward-facing persulfide intermediate on C364. Additional structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry and suggest a conserved β-hairpin structure plays a role in mediating interactions with SufE. These new structures, along with previous HDX-MS and biochemical data, identify an interaction network capable of communication between active-sites of the SufS dimer coordinating the shift between desulfurase and transpersulfurase activities.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.biochem.8b01122.

    • Size exclusion chromatogram of the R92A, E96A, and E250A SufS variants, heat map of atomic displacement parameters for the wild-type and E250A SufS structures, new interactions in SufS mutants at the dimer interface that drive dimer rearrangement, FoFc difference electron density in the vicinity of R92A, heat map of atomic displacement parameter values in the vicinity of C364 persulfide, and multiple sequence alignment of representative members of the SufS InterPro family IPR010970 (PDF)

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    The atomic coordinates and structure factors for E. coli SufS (P77444) wt with an inward-facing persulfide (6mr2), SufS H55A (6mr6), SufS R92A (6mre), SufS E96A (6mrh), and SufS E250A (6mri) have been deposited with the Protein Data Bank.

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    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

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