Linked Life Data

15781455

Source:http://linkedlifedata.com/resource/pubmed/id/15781455

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2005-5-23
pubmed:abstractText
Geobacillus tepidamans GS5-97(T) is a novel Gram-positive, moderately thermophilic bacterial species that is covered by a glycosylated surface layer (S-layer) protein. The isolated and purified S-layer glycoprotein SgtA was ultrastructurally and chemically investigated and showed several novel properties. By SDS-PAGE, SgtA was separated into four distinct bands in an apparent molecular mass range of 106-166 kDa. The three high molecular mass bands gave a positive periodic acid-Schiff staining reaction, whereas the 106-kDa band was nonglycosylated. Glycosylation of SgtA was investigated by means of chemical analyses, 600-MHz nuclear magnetic resonance spectroscopy, and electrospray ionization quadrupole time-of-fight mass spectrometry. Glycopeptides obtained after Pronase digestion revealed the glycan structure [-->2)-alpha-L-Rhap-(1-->3)-alpha-D-Fucp-(1-->](n=approximately 20), with D-fucopyranose having never been identified before as a constituent of S-layer glycans. The rhamnose residue at the nonreducing end of the terminal repeating unit of the glycan chain was di-substituted. For the first time, (R)-N-acetylmuramic acid, the key component of prokaryotic peptidoglycan, was found in an alpha-linkage to carbon 3 of the terminal rhamnose residue, serving as capping motif of an S-layer glycan. In addition, that rhamnose was substituted at position 2 with a beta-N-acetylglucosamine residue. The S-layer glycan chains were bound via the trisaccharide core -->2)-alpha-L-Rhap-(1-->3)-alpha-L-Rhap-(1-->3)-alpha-L-Rhap-(1--> to carbon 3 of beta-D-galactose, which was attached in O-glycosidic linkage to serine and threonine residues of SgtA of G. tepidamans GS5-97(T).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20292-9
pubmed:dateRevised
2008-9-18
pubmed:meshHeading
pubmed-meshheading:15781455-Bacillaceae, pubmed-meshheading:15781455-Carbohydrate Conformation, pubmed-meshheading:15781455-Carbohydrate Sequence, pubmed-meshheading:15781455-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15781455-Fucose, pubmed-meshheading:15781455-Galactose, pubmed-meshheading:15781455-Glycoproteins, pubmed-meshheading:15781455-Glycosylation, pubmed-meshheading:15781455-Magnetic Resonance Spectroscopy, pubmed-meshheading:15781455-Membrane Glycoproteins, pubmed-meshheading:15781455-Microscopy, Electron, pubmed-meshheading:15781455-Molecular Sequence Data, pubmed-meshheading:15781455-Muramic Acids, pubmed-meshheading:15781455-Polysaccharides, pubmed-meshheading:15781455-Pronase, pubmed-meshheading:15781455-Rhamnose, pubmed-meshheading:15781455-Sequence Analysis, pubmed-meshheading:15781455-Serine, pubmed-meshheading:15781455-Spectrometry, Mass, Electrospray Ionization, pubmed-meshheading:15781455-Threonine
pubmed:year
2005
pubmed:articleTitle
N-acetylmuramic acid as capping element of alpha-D-fucose-containing S-layer glycoprotein glycans from Geobacillus tepidamans GS5-97T.
pubmed:affiliation
Department of Organic Chemistry, University of Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't