Proteomics

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Chemical-crosslinking of SurA with DSBU to unfolded Omps (OmpA and OmpX)

ABSTRACT: To investigate the structural basis of SurA’s chaperone function, we characterized crosslinks between it and two of its clients, OmpA and OmpX, and used those as distance restraints to build structural models.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Escherichia Coli

TISSUE(S): Cell Culture

SUBMITTER: Stephen Fried  

LAB HEAD: Stephen Fried

PROVIDER: PXD021872 | Pride | 2020-10-29

REPOSITORIES: Pride

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Publications

SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins.

Marx Dagan C DC   Plummer Ashlee M AM   Faustino Anneliese M AM   Devlin Taylor T   Roskopf Michaela A MA   Leblanc Mathis J MJ   Lessen Henry J HJ   Amann Barbara T BT   Fleming Patrick J PJ   Krueger Susan S   Fried Stephen D SD   Fleming Karen G KG  

Proceedings of the National Academy of Sciences of the United States of America 20201022 45

The periplasmic chaperone network ensures the biogenesis of bacterial outer membrane proteins (OMPs) and has recently been identified as a promising target for antibiotics. SurA is the most important member of this network, both due to its genetic interaction with the β-barrel assembly machinery complex as well as its ability to prevent unfolded OMP (uOMP) aggregation. Using only binding energy, the mechanism by which SurA carries out these two functions is not well-understood. Here, we use a co  ...[more]

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