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Structure analysis of endosialidase NF at 0.98 Å resolution
Author(s) -
Schulz Eike C.,
Neumann Piotr,
GerardySchahn Rita,
Sheldrick George M.,
Ficner Ralf
Publication year - 2010
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444909048720
Subject(s) - resolution (logic) , computer science , artificial intelligence
Endosialidase NF (endoNF) is a bacteriophage‐derived endosialidase that specifically degrades α‐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 Å 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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