Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure analysis of endosialidase NF at 0.98 A resolution.,Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. Epub 2010 Jan 22. PMID:20124697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R. Structure analysis of endosialidase NF at 0.98 A resolution. Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. Epub 2010 Jan 22. PMID:20124697 doi:10.1107/S0907444909048720
