Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding
Copyright policy )Neisseria meningitidis Serogroup B Polysialyltransferase: Insights into Substrate Binding
On the loose: We report an STD NMR spectroscopic study of the polysialyltransferase from Neisseria meningitidis serogroup B (NmB-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 NmB-polyST that provide the basis for the development of novel NmB-polyST inhibitors.
- Hochschule Hannover Germany
- Griffith University Australia
- Hannover Medical School Germany
Binding Sites, Magnetic Resonance Spectroscopy, Biochemistry and cell biology, Recombinant Fusion Proteins, Medicinal and biomolecular chemistry, Medical biochemistry and metabolomics not elsewhere classified, Neisseria meningitidis, Serogroup B, N-Acetylneuraminic Acid, Sialyltransferases, Protein Binding
Binding Sites, Magnetic Resonance Spectroscopy, Biochemistry and cell biology, Recombinant Fusion Proteins, Medicinal and biomolecular chemistry, Medical biochemistry and metabolomics not elsewhere classified, Neisseria meningitidis, Serogroup B, N-Acetylneuraminic Acid, Sialyltransferases, Protein Binding
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