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PDBsum entry 2dde
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PDB id:
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Antibiotic
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Title:
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Structure of cinnamycin complexed with lysophosphatidylethanolamine
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Structure:
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Lantibiotic cinnamycin. Chain: a. Synonym: lanthiopeptin, lantibiotic ro 09- 0198
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Source:
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Streptomyces griseoverticillatus. Organism_taxid: 68215
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NMR struc:
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10 models
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Authors:
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K.Hosoda,M.Ohya,T.Kohno,T.Maeda,S.Endo,K.Wakamatsu
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Key ref:
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K.Hosoda
et al.
(1996).
Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.
J Biochem (tokyo),
119,
226-230.
PubMed id:
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Date:
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27-Jan-06
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Release date:
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21-Feb-06
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PROCHECK
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Headers
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References
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P29827
(CINA_STRGV) -
Lantibiotic cinnamycin from Streptomyces griseoverticillatus
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Seq:
Struc:
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78 a.a.
19 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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J Biochem (tokyo)
119:226-230
(1996)
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PubMed id:
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Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.
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K.Hosoda,
M.Ohya,
T.Kohno,
T.Maeda,
S.Endo,
K.Wakamatsu.
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ABSTRACT
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The three-dimensional structure of a complex of cinnamycin, a 19-amino acid
residue immunopotentiator peptide, and lysophosphatidylethanolamine was
determined by 1H-NMR. The complex was cylindrical in shape, 11 A in diameter and
26 A in length, excluding the acyl chain of the phospholipid. The peptide had a
hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the
head group of the ligand. Fitting of the head group to the hydrophobic pocket
was so good that other than a glycerophosphoethanolamine head group would be
unable to fit the pocket. The goodness of the fitting is compatible with the
strict specificity of ligand binding of the peptide.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.M.Willey,
and
W.A.van der Donk
(2007).
Lantibiotics: peptides of diverse structure and function.
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Annu Rev Microbiol,
61,
477-501.
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G.Machaidze,
and
J.Seelig
(2003).
Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine. Comparison between micellar and membrane environments.
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Biochemistry,
42,
12570-12576.
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M.Wada,
S.Nakamori,
and
H.Takagi
(2003).
Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity.
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FEMS Microbiol Lett,
225,
189-193.
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A.Guder,
I.Wiedemann,
and
H.G.Sahl
(2000).
Posttranslationally modified bacteriocins--the lantibiotics.
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Biopolymers,
55,
62-73.
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H.Brötz,
M.Josten,
I.Wiedemann,
U.Schneider,
F.Götz,
G.Bierbaum,
and
H.G.Sahl
(1998).
Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics.
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Mol Microbiol,
30,
317-327.
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H.G.Sahl,
and
G.Bierbaum
(1998).
Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria.
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Annu Rev Microbiol,
52,
41-79.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
