4G9S

Crystal structure of Escherichia coli PliG in complex with Atlantic salmon g-type lysozyme

Summary for 4G9S

• Entry DOI: 10.2210/pdb4g9s/pdb
• Descriptor: Goose-type lysozyme, Inhibitor of g-type lysozyme, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: hydrolase inhibitor, lysozyme, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Salmo salar (Atlantic salmon); More
• Cellular location: Periplasm: P76002
• Total number of polymer chains: 2
• Total formula weight: 33858.10

Authors

Leysen, S.,Vanderkelen, L.,Weeks, S.D.,Michiels, C.W.,Strelkov, S.V. (deposition date: 2012-07-24, release date: 2012-11-07, Last modification date: 2023-09-13)

Primary citation

Leysen, S.,Vanderkelen, L.,Weeks, S.D.,Michiels, C.W.,Strelkov, S.V.
Structural basis of bacterial defense against g-type lysozyme-based innate immunity.
Cell.Mol.Life Sci., 70:1113-1122, 2013

PubMed Abstract: Gram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor of g-type lysozyme (PliG-Ec) in complex with Atlantic salmon g-type lysozyme (SalG) at a resolution of 0.95 Å, which is exceptionally high for a complex of two proteins. The structure reveals for the first time the mechanism of g-type lysozyme inhibition by the PliG family. The latter contains two specific conserved regions that are essential for its inhibitory activity. The inhibitory complex formation is based on a double 'key-lock' mechanism. The first key-lock element is formed by the insertion of two conserved PliG regions into the active site of the lysozyme. The second element is defined by a distinct pocket of PliG accommodating a lysozyme loop. Computational analysis indicates that this pocket represents a suitable site for small molecule binding, which opens an avenue for the development of novel antibacterial agents that suppress the inhibitory activity of PliG.

PubMed: 23086131
DOI: 10.1007/s00018-012-1184-1

Experimental method

X-RAY DIFFRACTION (0.95 Å)