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Cover Picture: Defining a Substrate‐Binding Model of a Polysialyltransferase (ChemBioChem 15/2013)
Author(s) -
Freiberger Friedrich,
Böhm Raphael,
Schwarzer David,
GerardySchahn Rita,
Haselhorst Thomas,
von Itzstein Mark
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390054
Subject(s) - chemistry , binding site , cover (algebra) , acceptor , substrate (aquarium) , domain (mathematical analysis) , binding domain , stereochemistry , amino acid residue , biochemistry , peptide sequence , biology , ecology , gene , mechanical engineering , mathematical analysis , physics , mathematics , engineering , condensed matter physics
The cover picture shows the proposed PolySia acceptor and CMP‐Neu5Ac binding model of Neisseria meningitidis ( Nm ) polysialyltransferase (foreground) and Nm bacteria adhering to a cell surface (background). The polySia acceptor binding site is located within the first Rossmann domain and accommodates at least six Sia acceptor residues. The CMP‐Sia donor binding site is located within the second Rossmann domain. The key amino acid residues involved in either donor recognition or enzyme catalysis—H278, S328, S329 and E153—were identified in the two Rossmann Domains. For further information, see the communication by T. Haselhorst, M. von Itzstein, et al. on p. 1949 ff.