Cover Picture: Defining a Substrate‐Binding Model of a Polysialyltransferase (ChemBioChem 15/2013). Issue 15 (7th October 2013)

• Record Type: Journal Article
• Authors: Freiberger, Friedrich; Böhm, Raphael; Schwarzer, David; Gerardy‐Schahn, Rita; Haselhorst, Thomas; von Itzstein, Mark
• Is Part Of: Chembiochem. Volume 14:Issue 15(2013)
• Page Start: 1909
• Page End: 1909
• Publication Date: 2013-10-07
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201390054
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> the proposed PolySia acceptor and CMP‐Neu5Ac binding model of <italic>Neisseria meningitidis</italic> (<italic>Nm</italic>) polysialyltransferase (foreground) and <italic>Nm</italic> 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 <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 1949 ff.</ext-link><boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg3jxw6c4q" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>