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1v0e
From Proteopedia
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:17:46 2007'' |
Revision as of 15:12, 5 November 2007
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ENDOSIALIDASE OF BACTERIOPHAGE K1F
Overview
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.
About this Structure
1V0E is a Single protein structure of sequence from Xanthomonas phage cf16 with PO4 as ligand. Active as Endo-alpha-sialidase, with EC number 3.2.1.129 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F., Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R, Nat Struct Mol Biol. 2005 Jan;12(1):90-6. Epub 2004 Dec 19. PMID:15608653
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