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1v0e
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(New page: 200px<br /> <applet load="1v0e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v0e, resolution 1.90Å" /> '''ENDOSIALIDASE OF BA...)
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Revision as of 18:37, 29 October 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, ... [(full description)]
About this Structure
1V0E is a [Single protein] structure of sequence from [Bacteriophage k1f] with PO4 as [ligand]. Active as [[1]], with EC number [3.2.1.129]. 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
Page seeded by OCA on Mon Oct 29 20:42:18 2007
