5DN5

Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ

5DN5 の概要

• エントリーDOI: 10.2210/pdb5dn5/pdb
• 関連するPDBエントリー: 5DN4
• 分子名称: Peptidoglycan hydrolase FlgJ, IODIDE ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: glycoside hydrolase, family 73, flgj, flagella, hydrolase
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54138.19

構造登録者

Zaloba, P.,Bailey-Elkin, B.A.,Mark, B.L. (登録日: 2015-09-09, 公開日: 2016-02-24, 最終更新日: 2024-03-06)

主引用文献

Zaloba, P.,Bailey-Elkin, B.A.,Derksen, M.,Mark, B.L.
Structural and Biochemical Insights into the Peptidoglycan Hydrolase Domain of FlgJ from Salmonella typhimurium.
Plos One, 11:e0149204-e0149204, 2016

PubMed Abstract: FlgJ is a glycoside hydrolase (GH) enzyme belonging to the Carbohydrate Active enZyme (CAZy) family GH73. It facilitates passage of the bacterial flagellum through the peptidoglycan (PG) layer by cleaving the β-1,4 glycosidic bond between N-acetylglucosamine and N-acetylmuramic acid sugars that comprise the glycan strands of PG. Here we describe the crystal structure of the GH domain of FlgJ from bacterial pathogen Salmonella typhimurium (StFlgJ). Interestingly, the active site of StFlgJ was blocked by the C-terminal α-helix of a neighbouring symmetry mate and a β-hairpin containing the putative catalytic glutamic acid residue Glu223 was poorly resolved and could not be completely modeled into the electron density, suggesting it is flexible. Previous reports have shown that the GH73 enzyme Auto from Listeria monocytogenes is inhibited by an N-terminal α-helix that may occlude the active site in similar fashion. To investigate if the C-terminus of StFlgJ inhibits GH activity, the glycolytic activity of StFlgJ was assessed with and without the C-terminal α-helix. The GH activity of StFlgJ was unaffected by the presence or absence of the α-helix, suggesting it is not involved in regulating activity. Removal of the C-terminal α-helix did, however, allow a crystal structure of the domain to be obtained where the flexible β-hairpin containing residue Glu223 was entirely resolved. The β-hairpin was positioned such that the active site groove was fully solvent-exposed, placing Glu223 nearly 21.6 Å away from the putative general acid/base residue Glu184, which is too far apart for these two residues to coordinate glycosidic bond hydrolysis. The mobile nature of the StFlgJ β-hairpin is consistent with structural studies of related GH73 enzymes, suggesting that a dynamic active site may be common to many GH73 enzymes, in which the active site opens to capture substrate and then closes to correctly orient active site residues for catalysis.

PubMed: 26871950
DOI: 10.1371/journal.pone.0149204

実験手法

X-RAY DIFFRACTION (2.15 Å)