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Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding
Author(s) -
Böhm Raphael,
Freiberger Friedrich,
Stummeyer Katharina,
GerardySchahn Rita,
von Itzstein Mark,
Haselhorst Thomas
Publication year - 2010
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.200900659
Subject(s) - neisseria meningitidis , moiety , chemistry , neisseria , residue (chemistry) , cytosine , biochemistry , stereochemistry , microbiology and biotechnology , bacteria , biology , gene , genetics
On the loose: We report an STD NMR spectroscopic study of the polysialyltransferase from Neisseria meningitidis serogroup B ( Nm B‐polyST). The spectra reveal that the cytosine and ribose moiety receive more saturation than the sialic acid residue of CMP‐Neu5Ac. This loose binding enables a fast and efficient sialyl transfer to the acceptor substrate. Our analysis offers a view of the structural determinants necessary for binding to Nm B‐polyST that provide the basis for the development of novel Nm B‐polyST inhibitors.