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Endosialidase NF Appears To Bind PolySia DP5 in a Helical Conformation
Author(s) -
Haselhorst Thomas,
Stummeyer Katharina,
Mühlenhoff Martina,
Schaper Wiebke,
GerardySchahn Rita,
von Itzstein Mark
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600252
Subject(s) - chemistry , biophysics , biochemistry , crystallography , biology
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.