3GVK

Crystal structure of endo-neuraminidase NF mutant

3GVK の概要

• エントリーDOI: 10.2210/pdb3gvk/pdb
• 関連するPDBエントリー: 3GVJ
• 分子名称: Endo-N-acetylneuraminidase, N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-beta-neuraminic acid, N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-beta-neuraminic acid, ... (5 entities in total)
• 機能のキーワード: endo neuraminidase, polysialic acid, triple-beta helix, glycosidase, hydrolase
• 由来する生物種: Enterobacteria phage K1F (Bacteriophage K1F)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 230647.40

構造登録者

Schulz, E.C.,Dickmanns, A.,Ficner, R. (登録日: 2009-03-31, 公開日: 2010-03-02, 最終更新日: 2024-12-25)

主引用文献

Schulz, E.C.,Schwarzer, D.,Frank, M.,Stummeyer, K.,Muhlenhoff, M.,Dickmanns, A.,Gerardy-Schahn, R.,Ficner, R.
Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF.
J.Mol.Biol., 397:341-351, 2010

PubMed Abstract: An alpha-2,8-linked polysialic acid (polySia) capsule confers immune tolerance to neuroinvasive, pathogenic prokaryotes such as Escherichia coli K1 and Neisseria meningitidis and supports host infection by means of molecular mimicry. Bacteriophages of the K1 family, infecting E. coli K1, specifically recognize and degrade this polySia capsule utilizing tailspike endosialidases. While the crystal structure for the catalytic domain of the endosialidase of bacteriophage K1F (endoNF) has been solved, there is yet no structural information on the mode of polySia binding and cleavage available. The crystal structure of activity deficient active-site mutants of the homotrimeric endoNF cocrystallized with oligomeric sialic acid identified three independent polySia binding sites in each endoNF monomer. The bound oligomeric sialic acid displays distinct conformations at each site. In the active site, a Sia(3) molecule is bound in an extended conformation representing the enzyme-product complex. Structural and biochemical data supported by molecular modeling enable to propose a reaction mechanism for polySia cleavage by endoNF.

PubMed: 20096705
DOI: 10.1016/j.jmb.2010.01.028

実験手法

X-RAY DIFFRACTION (1.84 Å)