2hqs
From Proteopedia
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Crystal structure of TolB/Pal complex
Overview
We report the crystal structure of the Escherichia coli TolB-Pal complex, a protein-protein complex involved in maintaining the integrity of the, outer membrane (OM) in all Gram-negative bacteria that is parasitized by, colicins (protein antibiotics) to expedite their entry into cells., Nuclease colicins competitively recruit TolB using their natively, disordered regions (NDRs) to disrupt its complex with Pal, which is, thought to trigger translocation of the toxin across a locally, destabilized OM. The structure shows induced-fit binding of, peptidoglycan-associated lipoprotein (Pal) to the beta-propeller domain of, TolB causing the N-terminus of one of its alpha-helices to unwind and, several residues to undergo substantial changes in conformation. The, resulting interactions with TolB are known to be essential for the, stability of the complex and the bacterial OM. Structural comparisons with, a TolB-colicin NDR complex reveal that colicins bind at the Pal site, mimicking rearranged Pal residues while simultaneously appearing to block, induced-fit changes in TolB. The study therefore explains how colicins, recruit TolB in the bacterial periplasm and highlights a novel binding, mechanism for a natively disordered protein.
About this Structure
2HQS is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
Molecular mimicry enables competitive recruitment by a natively disordered protein., Bonsor DA, Grishkovskaya I, Dodson EJ, Kleanthous C, J Am Chem Soc. 2007 Apr 18;129(15):4800-7. Epub 2007 Mar 22. PMID:17375930
Page seeded by OCA on Wed Jan 23 15:30:36 2008
Categories: Escherichia coli | Protein complex | Bonsor, D.A. | Dodson, E.J. | Grishkovskaya, I. | Kleanthous, C. | ACT | GOL | SO4 | Pal | Tol | Tolb
