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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1996-11-4
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pubmed:abstractText |
In continuation of our studies on the structure and function of peptaibol antibiotics, the conformational properties of a sequence analogous to that of Trichodecenin I (Z-Gly-Gly-D-Leu-Aib-Gly-D-Ile-D-Leu-OMe, where Z = benzyloxycarbonyl, Aib = alpha-aminoisobutyric acid, and OMe = methyl ester) have been investigated crystallographically. This sequence is the mirror image of the naturally occurring molecule and also of the C-terminal heptapeptide of the related lipopeptaibol Trichogin A IV (where, however, the Leu-OMe residue has replaced the original Leuol residue). The molecule crystallized in the monoclinic system, space group P21, Z = 4, and cell parameters a = 11.610(5), b = 33.342(8), c = 11.735(4) A, beta = 110.42(1) degrees, V = 4257(3) A3. The crystallographic refinement converges at residual values of R = 0.047 and wR2 = 0.134 on F2. In the 1-5 segment the molecular conformation is virtually identical to that one reported from solution nmr studies of a similarly protected sequence [Biopolymers (1995), Vol. 35. pp. 21-29)] and is characterized by beta-turns of type I at Gly1-Gly2, II' at Leu3-Aib4, and I at Aib4-Gly5. In the crystal structure, a beta-sheet-like arrangement is seen at the C-terminus.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Infective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/trichodecenin I,
http://linkedlifedata.com/resource/pubmed/chemical/trichogin A IV
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3525
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31-42
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8924625-Anti-Bacterial Agents,
pubmed-meshheading:8924625-Anti-Infective Agents,
pubmed-meshheading:8924625-Crystallography, X-Ray,
pubmed-meshheading:8924625-Fatty Acids, Unsaturated,
pubmed-meshheading:8924625-Hydrogen Bonding,
pubmed-meshheading:8924625-Lipopeptides,
pubmed-meshheading:8924625-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8924625-Models, Molecular,
pubmed-meshheading:8924625-Oligopeptides,
pubmed-meshheading:8924625-Peptides,
pubmed-meshheading:8924625-Protein Conformation,
pubmed-meshheading:8924625-Protein Structure, Secondary
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pubmed:year |
1996
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pubmed:articleTitle |
Crystallographic structure of a multiple beta-turn containing, glycine-rich heptapeptide: a synthetic precursor of the lipopeptaibol antibiotic trichodecenin I.
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pubmed:affiliation |
Department of Organic Chemistry, University of Padova, Italy.
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pubmed:publicationType |
Journal Article
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