1V0F

Endosialidase of Bacteriophage K1F in complex with oligomeric alpha-2,8-sialic acid

1V0F の概要

• エントリーDOI: 10.2210/pdb1v0f/pdb
• 関連するPDBエントリー: 1V0E
• 分子名称: ENDO-ALPHA-SIALIDASE, N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-alpha-neuraminic acid, N-acetyl-beta-neuraminic acid, ... (5 entities in total)
• 機能のキーワード: endosialidase, polysialic acid degradation, hydrolase, glycosidase.
• 由来する生物種: COLIPHAGE K1F
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 449018.84

構造登録者

Stummeyer, K.,Dickmanns, A.,Muehlenhoff, M.,Gerady-Schahn, R.,Ficner, R. (登録日: 2004-03-28, 公開日: 2004-12-13, 最終更新日: 2024-05-08)

主引用文献

Stummeyer, K.,Dickmanns, A.,Muehlenhoff, M.,Gerardy-Schahn, R.,Ficner, R.
Crystal Structure of the Polysialic Acid-Degrading Endosialidase of Bacteriophage K1F
Nat.Struct.Mol.Biol., 12:90-, 2005

PubMed Abstract: Phages infecting the polysialic acid (polySia)-encapsulated human pathogen Escherichia coli K1 are equipped with capsule-degrading tailspikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. As polySia also promotes cellular plasticity and tumor metastasis in vertebrates, endosialidases are widely applied in polySia-related neurosciences and cancer research. Here we report the crystal structures of endosialidase NF and its complex with oligomeric sialic acid. The structure NF, which reveals three distinct domains, indicates that the unique polySia specificity evolved from a combination of structural elements characteristic of exosialidases and bacteriophage tailspike proteins. The endosialidase assembles into a catalytic trimer stabilized by a triple beta-helix. Its active site differs markedly from that of exosialidases, indicating an endosialidase-specific substrate-binding mode and catalytic mechanism. Residues essential for endosialidase activity were identified by structure-based mutational analysis.

PubMed: 15608653
DOI: 10.1038/NSMB874

実験手法

X-RAY DIFFRACTION (2.55 Å)