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9BIY

Crystal structure of the periplasmic domain of IgaA from Escherichia coli

Summary for 9BIY
Entry DOI10.2210/pdb9biy/pdb
DescriptorIntracellular growth attenuator protein igaA, Outer membrane lipoprotein RcsF (3 entities in total)
Functional Keywordsperiplasmic protein, signal transduction, structural genomics, center for structural biology of infectious diseases, csbid, center for structural genomics of infectious diseases, csgid, signaling protein
Biological sourceEscherichia coli
More
Total number of polymer chains2
Total formula weight39231.57
Authors
Primary citationWatanabe, N.,Savchenko, A.
Molecular insights into the initiation step of the Rcs signaling pathway.
Structure, 32:1381-, 2024
Cited by
PubMed Abstract: The Rcs pathway is repressed by the inner membrane protein IgaA under non-stressed conditions. This repression is hypothesized to be relieved by the binding of the outer membrane-anchored RcsF to IgaA. However, the precise mechanism by which RcsF binding triggers the signaling remains unclear. Here, we present the 1.8 Å resolution crystal structure capturing the interaction between IgaA and RcsF. Our comparative structural analysis, examining both the bound and unbound states of the periplasmic domain of IgaA (IgaAp), highlights rotational flexibility within IgaAp. Conversely, the conformation of RcsF remains unchanged upon binding. Our in vivo and in vitro studies do not support the model of a stable complex involving RcsF, IgaAp, and RcsDp. Instead, we demonstrate that the elements beyond IgaAp play a role in the interaction between IgaA and RcsD. These findings collectively allow us to propose a potential mechanism for the signaling across the inner membrane through IgaA.
PubMed: 38964336
DOI: 10.1016/j.str.2024.06.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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PDB entries from 2024-11-20

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