Structural characterization of the PliG lysozyme inhibitor family

Several Gram-negative bacteria protect themselves against the lytic action of host lysozymes by producing specific proteinaceous inhibitors. So far, four different families of lysozyme inhibitors have been identified including Ivy (Inhibitor of vertebrate lysozyme), MliC/PliC (Membrane associated/pe...

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Vydané v:	Journal of structural biology Ročník 180; číslo 1; s. 235 - 242
Hlavní autori:	Leysen, Seppe, Vanderkelen, Lise, Van Asten, Kathleen, Vanheuverzwijn, Steven, Theuwis, Veronique, Michiels, Chris W., Strelkov, Sergei V.
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States Elsevier Inc 01.10.2012
Predmet:	Aeromonas hydrophila Amino Acid Sequence Amino Acid Substitution Conserved Sequence Crystal structure Crystallography, X-Ray Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Lysozyme Lysozyme inhibitors Models, Molecular Molecular Sequence Data Muramidase - antagonists & inhibitors Muramidase - chemistry Mutagenesis, Site-Directed PliG Protein Interaction Domains and Motifs Protein Structure, Quaternary Protein Structure, Secondary Salmonella typhimurium SAXS Structural Homology, Protein Lysozyme inhibitors PliG Lysozyme Crystal structure SAXS
ISSN:	1047-8477, 1095-8657, 1095-8657
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Shrnutí:	Several Gram-negative bacteria protect themselves against the lytic action of host lysozymes by producing specific proteinaceous inhibitors. So far, four different families of lysozyme inhibitors have been identified including Ivy (Inhibitor of vertebrate lysozyme), MliC/PliC (Membrane associated/periplasmic inhibitor of C-type lysozyme), PliI and PliG (periplasmic inhibitors of I- and G-type lysozymes, respectively). Here we provide the first crystallographic description of the PliG family. Crystal structures were obtained for the PliG homologues from Escherichia coli, Salmonella enterica serotype Typhimurium and Aeromonas hydrophila. These structures show that the fold of the PliG family is very distinct from that of all other families of lysozyme inhibitors. Small-angle X-ray scattering studies reveal that PliG is monomeric in solution as opposed to the dimeric PliC and PliI. The PliG family shares a highly conserved SG(x)xY sequence motif with the MliC/PliC and PliI families where it was shown to reside on a loop that blocks the active site of lysozyme leading to inhibition. Surprisingly, we found that in PliG this motif is not well exposed and not involved in the inhibitory action. Instead, we could identify a distinct cluster of surface residues that are conserved across the PliG family and are essential for efficient G-type lysozyme inhibition, as evidenced by mutagenesis studies.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1047-8477 1095-8657 1095-8657
DOI:	10.1016/j.jsb.2012.05.006