5Z38

Crystal structure of CsrA bound to CesT

Summary for 5Z38

• Entry DOI: 10.2210/pdb5z38/pdb
• Descriptor: CesT protein, Truncated-CsrA, wild type CsrA, ... (4 entities in total)
• Functional Keywords: ehec and epec, rna binding protein-chaperone complex, rna binding protein/chaperone
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : B7UHB4 B7UHB4
• Total number of polymer chains: 12
• Total formula weight: 122302.49

Authors

Ye, F.,Yang, F.,Yu, R.,Lin, X.,Qi, J.,Chen, Z.,Gao, G.F.,Lu, G. (deposition date: 2018-01-05, release date: 2018-04-04, Last modification date: 2023-11-22)

Primary citation

Ye, F.,Yang, F.,Yu, R.,Lin, X.,Qi, J.,Chen, Z.,Cao, Y.,Wei, Y.,Gao, G.F.,Lu, G.
Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
Nat Commun, 9:1196-1196, 2018

PubMed Abstract: The T3SS chaperone CesT is recently shown to interact with the post-transcriptional regulator CsrA to modulate post-attachment signaling in enteropathogenic and enterohemorrhagic Escherichia coli. The molecular basis of the CesT/CsrA binding, however, remains elusive. Here, we show that CesT and CsrA both created two ligand binding sites in their homodimers, forming irregular multimeric complexes in solution. Through construction of a recombinant CsrA-dimer (Re-CsrA) that contains a single CesT binding site, the atomic binding features between CesT and CsrA are delineated via the structure of the CesT/Re-CsrA complex. In contrast to a previously reported N-terminally swapped dimer-form, CesT adopts a dimeric architecture with a swapped C-terminal helix for CsrA engagement. In CsrA, CesT binds to a surface patch that extensively overlaps with its mRNA binding site. The binding mode therefore justifies a mechanism of CsrA-modulation by CesT via competitive inhibition of the CsrA/mRNA interactions.

PubMed: 29567971
DOI: 10.1038/s41467-018-03625-x

Experimental method

X-RAY DIFFRACTION (2.292 Å)