Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1991-12-11
|
pubmed:abstractText |
The 21-peptide amide antibiotic gallidermin is a potential therapeutic against acne disease. It belongs to the class of polycyclic lanthionine and alpha,beta-didehydroamino acids containing polypeptides, which were named "lantibiotics." The structural gene of the recently elucidated lantibiotic gallidermin encodes a precursor peptide containing Ser, Thr, and Cys residues in the C-terminal prolantibiotic part, and an unusually hydrophilic leader peptide. The ribosomally synthesized pregallidermin is posttranslationally modified and processed to a complex peptide antibiotic with four sulfide rings and two unsaturated residues. The complete solution structure of gallidermin was determined in trifluoroethanol: water (95:5) and dimethylsulfoxide by two-dimensional 1H-nmr at 500 MHz, using a combination of double quantum filtered correlated spectroscopy, homonuclear Hartman-Hahn, and nuclear Overhauser enhancement spectroscopy experiments. Using a total number of 152 distance constraints from NOEs and 14 torsional constraints, derived from coupling constants, we obtained a screwlike solution structure of gallidermin. Restrained molecular dynamics simulations yielded a set of five converging structures with an atomic rms difference of 1.7 A for the backbone atoms, not dependent on the starting structure. The spatial structure model is in excellent agreement with the amphiphilic and channel-forming properties of gallidermin on membranes and its tryptic cleavage at the exposed site between residues 13 and 14.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacteriocins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/gallidermin
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-3525
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
31
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
803-11
|
pubmed:dateRevised |
2005-11-17
|
pubmed:meshHeading |
pubmed-meshheading:1932575-Anti-Bacterial Agents,
pubmed-meshheading:1932575-Bacteriocins,
pubmed-meshheading:1932575-Circular Dichroism,
pubmed-meshheading:1932575-Hydrogen Bonding,
pubmed-meshheading:1932575-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1932575-Models, Molecular,
pubmed-meshheading:1932575-Peptides,
pubmed-meshheading:1932575-Peptides, Cyclic,
pubmed-meshheading:1932575-Solutions,
pubmed-meshheading:1932575-Temperature
|
pubmed:year |
1991
|
pubmed:articleTitle |
The solution structure of the lantibiotic gallidermin.
|
pubmed:affiliation |
Institut für Organische Chemie, Universität Tübingen, Federal Republic of Germany.
|
pubmed:publicationType |
Journal Article
|