3ju4
Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution
Structural highlights
FunctionFIBER_BPK1F Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.[1] [2] The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.[3] 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 PubMedEndosialidase 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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