Endosialidase NF Appears To Bind PolySia DP5 in a Helical Conformation
Author(s)
Haselhorst, Thomas
Stummeyer, Katharina
Muehlenhoff, Martina
Schaper, Wiebke
Gerardy-Schahn, Rita
von Itzstein, Mark
Year published
2006
Metadata
Show full item recordAbstract
Phages infecting the polySia-encapsulated human pathogen E. coli K1 are equipped with capsule-degrading tail spikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. The X-ray crystallographic structure of endosialidase has been reported but it remains unclear how polySia interacts with the active site. Here we report STD and trNOE NMR experiments that investigate the binding mode of polySia DP5 at a molecular level.Phages infecting the polySia-encapsulated human pathogen E. coli K1 are equipped with capsule-degrading tail spikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. The X-ray crystallographic structure of endosialidase has been reported but it remains unclear how polySia interacts with the active site. Here we report STD and trNOE NMR experiments that investigate the binding mode of polySia DP5 at a molecular level.
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Journal Title
ChemBioChem
Volume
7
Publisher URI
Copyright Statement
© 2006 John Wiley & Sons, Ltd. Self-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the author for more information.
Subject
Medicinal and Biomolecular Chemistry
Biochemistry and Cell Biology