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Figure 2
Cysteine modification reorganizes non-covalent interaction networks similar to on-pathway catalytic intermediates. The graph networks depict a protein structure, with nodes representing residues, solid lines representing covalent bonds, and dashed lines representing non-covalent interactions. A reactive thiol­ate can be covalently modified through binding a substrate, or by a transient reaction intermediate. The covalent modification neutralizes the charge on the Sγ atom, changing the electrostatic microenvironment of the active site. X-ray induced photooxidation of Cys-S− to Cys-SOH equally results in thiol­ate charge neutralization. The modified charge of the Sγ acceptor atom considerably weakens or even disrupts any hydrogen bond. This altered non-covalent network can redistribute the protein conformational ensemble well beyond the active site microenvironment.

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 26| Part 4| July 2019| Pages 958-966
https://doi.org/10.1107/S160057751900568X
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