1V0E

Endosialidase of Bacteriophage K1F

Summary for 1V0E

• Entry DOI: 10.2210/pdb1v0e/pdb
• Related: 1V0F
• Descriptor: ENDO-ALPHA-SIALIDASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: endosialidase, polysialic acid degradation, hydrolase, glycosidase.
• Biological source: COLIPHAGE K1F
• Total number of polymer chains: 6
• Total formula weight: 445361.64

Authors

Stummeyer, K.,Dickmanns, A.,Muehlenhoff, M.,Gerady-Schahn, R.,Ficner, R. (deposition date: 2004-03-28, release date: 2004-12-13, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)