3OD9

Crystal structure of PliI-Ah, periplasmic lysozyme inhibitor of I-type lysozyme from Aeromonas hydrophyla

3OD9 の概要

• エントリーDOI: 10.2210/pdb3od9/pdb
• 分子名称: Putative exported protein, POTASSIUM ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: beta sandwich, c-terminal helix, hydrolase inhibitor
• 由来する生物種: Aeromonas hydrophila
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44378.77

構造登録者

Leysen, S.,Van Herreweghe, J.M.,Callewaert, L.,Heirbaut, M.,Buntinx, P.,Michiels, C.W.,Strelkov, S.V. (登録日: 2010-08-11, 公開日: 2010-12-22, 最終更新日: 2024-02-21)

主引用文献

Leysen, S.,Van Herreweghe, J.M.,Callewaert, L.,Heirbaut, M.,Buntinx, P.,Michiels, C.W.,Strelkov, S.V.
Molecular Basis of Bacterial Defense against Host Lysozymes: X-ray Structures of Periplasmic Lysozyme Inhibitors PliI and PliC.
J.Mol.Biol., 405:1233-1245, 2011

PubMed Abstract: Lysozymes play a key role in the innate immune system of vertebrates and invertebrates by hydrolyzing peptidoglycan, a vital component of the bacterial cell wall. Gram-negative bacteria produce various types of lysozyme inhibitors that allow them to survive the bactericidal action of lysozyme when their outer membrane is permeabilized. So far, three lysozyme inhibitor families have been described: the Ivy (inhibitor of vertebrate lysozyme) family, the MliC/PliC (membrane-associated/periplasmic lysozyme inhibitor of C-type lysozyme) family, and the PliI (periplasmic lysozyme inhibitor of I-type lysozyme) family. Here, we report high-resolution crystal structures of Salmonella typhimurium PliC (PliC-St) and Aeromonas hydrophila PliI (PliI-Ah). The structure of PliI-Ah is the first in the recently discovered PliI family of lysozyme inhibitors, while the structure of PliC-St is the first structure of a periplasmic lysozyme inhibitor from the PliC/MliC family. Using small-angle X-ray scattering, we demonstrate that both PliC-St and PliI-Ah form stable dimers in solution. The functional dimer architecture of PliC-St is very different from that of the recently described MliC from Pseudomonas aeruginosa (MliC-Pa), despite the close resemblance of their monomers. Furthermore, PliI-Ah has distinctly different monomer and dimer folds compared to PliC, MliC, and Ivy proteins. Site-directed mutagenesis suggests that the inhibitory action of PliI-Ah proceeds via an insertion of a loop containing the conserved SGxY motif into the active center of I-type lysozymes. This motif is related to the functional SGxxY motif found in the MliC/PliC family.

PubMed: 21146533
DOI: 10.1016/j.jmb.2010.12.007

実験手法

X-RAY DIFFRACTION (1.411 Å)