Affordable Access

deepdyve-link
Publisher Website

Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme.

Authors
  • Kyomuhendo, Peter
  • Nilsen, Inge W
  • Brandsdal, Bjørn Olav
  • Smalås, Arne O
Type
Published Article
Journal
Journal of Molecular Modeling
Publisher
Springer-Verlag
Publication Date
Sep 01, 2008
Volume
14
Issue
9
Pages
777–788
Identifiers
DOI: 10.1007/s00894-008-0317-9
PMID: 18491152
Source
Medline
License
Unknown

Abstract

It is known that bacteria contain inhibitors of lysozyme activity. The recently discovered Escherichia coli inhibitor of vertebrate lysozyme (Ivy) and its potential interactions with several goose-type (g-type) lysozymes from fish were studied using functional enzyme assays, comparative homology modelling, protein-protein docking, and molecular dynamics simulations. Enzyme assays carried out on salmon g-type lysozyme revealed a lack of inhibition by Ivy. Detailed analysis of the complexes formed between Ivy and both hen egg white lysozyme (HEWL) and goose egg white lysozyme (GEWL) suggests that electrostatic interactions make a dominant contribution to inhibition. Comparison of three dimensional models of aquatic g-type lysozymes revealed important insertions in the beta domain, and specific sequence substitutions yielding altered electrostatic surface properties and surface curvature at the protein-protein interface. Thus, based on structural homology models, we propose that Ivy is not effective against any of the known fish g-type lysozymes. Docking studies suggest a weaker binding mode between Ivy and GEWL compared to that with HEWL, and our models explain the mechanistic necessity for conservation of a set of residues in g-type lysozymes as a prerequisite for inhibition by Ivy.

Report this publication

Statistics

Seen <100 times