Source:http://linkedlifedata.com/resource/pubmed/id/20124697
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 2
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| pubmed:dateCreated |
2010-2-3
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| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1399-0047
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
66
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
176-80
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| pubmed:meshHeading |
pubmed-meshheading:20124697-Bacteriophages,
pubmed-meshheading:20124697-Catalytic Domain,
pubmed-meshheading:20124697-Crystallography, X-Ray,
pubmed-meshheading:20124697-Enzyme Stability,
pubmed-meshheading:20124697-Models, Molecular,
pubmed-meshheading:20124697-N-Acetylneuraminic Acid,
pubmed-meshheading:20124697-Neuraminidase,
pubmed-meshheading:20124697-Protein Multimerization,
pubmed-meshheading:20124697-Protein Structure, Quaternary,
pubmed-meshheading:20124697-Protein Structure, Tertiary
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| pubmed:year |
2010
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| pubmed:articleTitle |
Structure analysis of endosialidase NF at 0.98 A resolution.
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| pubmed:affiliation |
Abteilung für Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
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| pubmed:publicationType |
Journal Article
|