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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-4-24
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pubmed:abstractText |
Recently, the design of beta-sheet proteins and concomitant folding studies have attracted increasing attention. A unique natural all-beta domain occurs in a family of cytolytic bacterial toxins, the so-called RTX toxins. This domain consists of a variable number (about 6-45) of tandem repeats of a glycine-rich nine-residue motif with the consensus sequence GGXGXDX(L/I/F)X. The analysis of the three-dimensional structure of alkaline protease from Pseudomonas aeruginosa which possesses six of these repeats revealed that they fold into a novel 'parallel beta-roll' where calcium is bound within the turns connecting the beta-strands. A 75-mer peptide of the sequence NH(2)-WLS-[GGSGNDNLS](8)-COOH was chemically synthesised. Circular dichroism spectroscopy showed that this polypeptide folds in the presence of Ca(2+) and polyethylene glycol into a beta-structure which is presumably identical with the parallel beta-roll. This synthetic beta-roll behaves similarly to the isolated beta-roll domains from Escherichia coli haemolysin or Bordetella pertussis cyclolysin in terms of calcium binding and polymerisation behaviour.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Hemolysin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hlya protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Pseudomonas serine proteinase,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
470
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10734229-Adenylate Cyclase Toxin,
pubmed-meshheading:10734229-Amino Acid Motifs,
pubmed-meshheading:10734229-Amino Acid Sequence,
pubmed-meshheading:10734229-Bacterial Proteins,
pubmed-meshheading:10734229-Bacterial Toxins,
pubmed-meshheading:10734229-Biopolymers,
pubmed-meshheading:10734229-Calcium,
pubmed-meshheading:10734229-Circular Dichroism,
pubmed-meshheading:10734229-Consensus Sequence,
pubmed-meshheading:10734229-Escherichia coli Proteins,
pubmed-meshheading:10734229-Glycine,
pubmed-meshheading:10734229-Hemolysin Proteins,
pubmed-meshheading:10734229-Kinetics,
pubmed-meshheading:10734229-Models, Molecular,
pubmed-meshheading:10734229-Molecular Sequence Data,
pubmed-meshheading:10734229-Peptide Fragments,
pubmed-meshheading:10734229-Polyethylene Glycols,
pubmed-meshheading:10734229-Protein Folding,
pubmed-meshheading:10734229-Protein Precursors,
pubmed-meshheading:10734229-Protein Structure, Secondary,
pubmed-meshheading:10734229-Protein Structure, Tertiary,
pubmed-meshheading:10734229-Repetitive Sequences, Amino Acid,
pubmed-meshheading:10734229-Serine Endopeptidases,
pubmed-meshheading:10734229-Solubility
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pubmed:year |
2000
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pubmed:articleTitle |
Folding of a synthetic parallel beta-roll protein.
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pubmed:affiliation |
Institut für Biotechnologie der Martin-Luther-Universität Halle, Kurt-Mothes Strasse 3, D-06120, Halle/Saale, Germany. lilie@biochemtech.uni-halle.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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