Literature DB >> 20124697

Structure analysis of endosialidase NF at 0.98 A resolution.

Eike C Schulz1, Piotr Neumann, Rita Gerardy-Schahn, George M Sheldrick, Ralf Ficner.   

Abstract

Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.

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Year:  2010        PMID: 20124697     DOI: 10.1107/S0907444909048720

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


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