3JU4

Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution

Summary for 3JU4

• Entry DOI: 10.2210/pdb3ju4/pdb
• Related: 1V0E 1V0F
• Descriptor: Endo-N-acetylneuraminidase, N-acetyl-beta-neuraminic acid, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: endonf, polysia, high-resolution, 1a, glycosidase, hydrolase
• Biological source: Enterobacteria phage K1F (Bacteriophage K1F)
• Total number of polymer chains: 1
• Total formula weight: 75051.99

Authors

Schulz, E.C.,Neuman, P.,Gerardy-Schahn, R.,Sheldrick, G.M.,Ficner, R. (deposition date: 2009-09-14, release date: 2010-02-02, Last modification date: 2023-11-01)

Primary citation

Schulz, E.C.,Neumann, P.,Gerardy-Schahn, R.,Sheldrick, G.M.,Ficner, R.
Structure analysis of endosialidase NF at 0.98 A resolution.
Acta Crystallogr.,Sect.D, 66:176-180, 2010

PubMed 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.

PubMed: 20124697
DOI: 10.1107/S0907444909048720

Experimental method

X-RAY DIFFRACTION (0.98 Å)