Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: meningitis [ICD11:
1D01 
];
infection due to Neisseria meningitidis [ICD11:
XN1DV ]
The structure was elucidated in this paperNCBI PubMed ID: 19998304Publication DOI: 10.1002/cbic.200900659Journal NLM ID: 100937360Publisher: Weinheim, Germany: Wiley Interscience
Correspondence: t.haselhorst
griffith.edu.au; m.vonitzstein
griffith.edu.au
Institutions: Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222 (Australia), Fax: (+61) 7-555-28098
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.
Neisseria meningitidis, polysialyltransferase, STD NMR spectroscopy
Structure type: oligomer
Location inside paper: p.72, fig.2 DP3
Trivial name: polysialic acid
Compound class: CPS
Contained glycoepitopes: IEDB_136794,IEDB_146100,IEDB_149174,IEDB_150072,IEDB_150937,IEDB_153199,IEDB_558870,IEDB_983929,SB_170,SB_171,SB_172,SB_35,SB_42,SB_84
Methods: X-ray, NMR-1D, biochemical methods, STD NMR
NCBI Taxonomy refs (TaxIDs): 491Reference(s) to other database(s): GTC:G57784EB
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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