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3ju4

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3ju4, resolution 0.98Å ()
Ligands: , ,
Activity: Endo-alpha-sialidase, with EC number 3.2.1.129
Related: 1v0e, 1v0f
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3ju4 is a 1 chain structure with sequence from Enterobacteria phage k1f. Full crystallographic information is available from OCA.

See Also

Reference

  • 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

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