Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation

van den Bedem, Henry; Wilson, Mark A.

doi:10.1107/s160057751900568x

Title: Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation

Journal Article · Thu Jun 13 00:00:00 EDT 2019 · Journal of Synchrotron Radiation (Online)

DOI:https://doi.org/10.1107/s160057751900568x· OSTI ID:1546912

^[1]; Wilson, Mark A. ^[2]

SLAC National Accelerator Lab., Menlo Park, CA (United States); Stanford Univ., CA (United States); Univ. of California, San Francisco, CA (United States)
Univ. of Nebraska, Lincoln, NE (United States)

We report that cysteine is a rare but functionally important amino acid that is often subject to covalent modification. Cysteine oxidation plays an important role in many human disease processes, and basal levels of cysteine oxidation are required for proper cellular function. Because reactive cysteine residues are typically ionized to the thiolate anion (Cys-S^-), their formation of a covalent bond alters the electrostatic and steric environment of the active site. X-ray-induced photo-oxidation to sulfenic acids (Cys-SOH) can recapitulate some aspects of the changes that occur under physiological conditions. Here we propose how site-specific cysteine photo-oxidation can be used to interrogate ensuing changes in protein structure and dynamics at atomic resolution. Although this powerful approach can connect cysteine covalent modification to global protein conformational changes and function, careful biochemical validation must accompany all such studies to exclude misleading artifacts. Lastly, new types of X-ray crystallography experiments and powerful computational methods are creating new opportunities to connect conformational dynamics to catalysis for the large class of systems that use covalently modified cysteine residues for catalysis or regulation.

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Research Organization:: SLAC National Accelerator Lab., Menlo Park, CA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1546912

Journal Information:: Journal of Synchrotron Radiation (Online), Vol. 26, Issue 4; ISSN 1600-5775

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
cysteine modification
radiation-controlled photo-oxidation
serial X-ray crystallography
enzyme conformational dynamics
molecular dynamics simulations

Title: Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation

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