1XS0

Structure of the E. coli Ivy protein

Summary for 1XS0

• Entry DOI: 10.2210/pdb1xs0/pdb
• Related: 1GPQ 1HKE
• Descriptor: Inhibitor of vertebrate lysozyme (2 entities in total)
• Functional Keywords: alpha beta fold, dimer, hydrolase inhibitor
• Biological source: Escherichia coli
• Cellular location: Periplasm: P45502
• Total number of polymer chains: 3
• Total formula weight: 45182.50

Authors

Abergel, C.,Monchois, V.,Byrn, D.,Lazzaroni, J.C.,Claverie, J.M. (deposition date: 2004-10-18, release date: 2004-11-02, Last modification date: 2024-10-30)

Primary citation

Abergel, C.,Monchois, V.,Byrne, D.,Chenivesse, S.,Lembo, F.,Lazzaroni, J.C.,Claverie, J.M.
Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria.
Proc.Natl.Acad.Sci.USA, 104:6394-6399, 2007

PubMed Abstract: Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antilysozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such, Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates.

PubMed: 17405861
DOI: 10.1073/pnas.0611019104

Experimental method

X-RAY DIFFRACTION (1.58 Å)