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PDBsum entry 1e68
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PDB id:
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Antibiotic
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Title:
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Solution structure of bacteriocin as-48
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Structure:
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As-48 protein. Chain: a. Fragment: bacteriocin as-48, residues 36-105. Synonym: bacteriocin as-4, peptide antibiotic as-48. Other_details: peptide link between residues 1 and 70
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Source:
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Enterococcus faecalis. Organism_taxid: 1351. Plasmid: pmb2
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NMR struc:
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20 models
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Authors:
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C.Gonzalez,G.Langdon,M.Bruix,A.Galvez,E.Valdivia,M.Maqueda,M.Rico
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Key ref:
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C.González
et al.
(2000).
Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.
Proc Natl Acad Sci U S A,
97,
11221-11226.
PubMed id:
DOI:
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Date:
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09-Aug-00
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Release date:
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25-Oct-00
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PROCHECK
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Headers
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References
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Q47765
(Q47765_ENTFL) -
AS-48 protein from Enterococcus faecalis
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Seq:
Struc:
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105 a.a.
70 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Proc Natl Acad Sci U S A
97:11221-11226
(2000)
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PubMed id:
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Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.
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C.González,
G.M.Langdon,
M.Bruix,
A.Gálvez,
E.Valdivia,
M.Maqueda,
M.Rico.
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ABSTRACT
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The solution structure of bacteriocin AS-48, a 70-residue cyclic polypeptide
from Enterococcus faecalis, consists of a globular arrangement of five
alpha-helices enclosing a compact hydrophobic core. The head-to-tail union lies
in the middle of helix 5, a fact that is shown to have a pronounced effect on
the stability of the three-dimensional structure. Positive charges in the side
chains of residues in helix 4 and in the turn linking helix 4 to helix 5 form a
cluster that most probably determine its antibacterial activity by promoting
pore formation in cell membranes. A similar five-helix structural motif has been
found in the antimicrobial NK-lysin, an effector polypeptide of T and natural
killer (NK) cells. Bacteriocin AS-48 lacks the three disulfide bridges
characteristic of the saposin fold present in NK-lysin, and has no sequence
homology with it. Nevertheless, the similar molecular architecture and high
positive charge strongly suggest a common mechanism of antibacterial action.
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Selected figure(s)
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Figure 1.
Fig. 1. Stereoscopic view of the superposition of the 20
best structures of bacteriocin AS-48, resulting from the DYANA
calculation. In black: superposition of backbone atoms. In red:
superposition of hydrophobic side chains at the core of the
structure. The figure was drawn with the program MOLSCRIPT.
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Figure 5.
Fig. 5. Front view (same orientation as in Fig. 4) and
back view (generated by a rotation of 180° around the z
axis) showing in cyan the hydrophobic regions at the surface of
bacteriocin AS-48.
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Figures were
selected
by an automated process.
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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.L.Neira,
L.M.Contreras,
O.R.de los Paños,
M.Sánchez-Hidalgo,
M.Martínez-Bueno,
M.Maqueda,
and
M.Rico
(2010).
Structural characterisation of the natively unfolded enterocin EJ97.
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Protein Eng Des Sel,
23,
507-518.
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L.Cascales,
and
D.J.Craik
(2010).
Naturally occurring circular proteins: distribution, biosynthesis and evolution.
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Org Biomol Chem,
8,
5035-5047.
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R.Renthal
(2010).
Helix insertion into bilayers and the evolution of membrane proteins.
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Cell Mol Life Sci,
67,
1077-1088.
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J.A.McIntosh,
M.S.Donia,
and
E.W.Schmidt
(2009).
Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.
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Nat Prod Rep,
26,
537-559.
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L.A.Martin-Visscher,
X.Gong,
M.Duszyk,
and
J.C.Vederas
(2009).
The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif.
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J Biol Chem,
284,
28674-28681.
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PDB code:
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M.R.Beck,
G.T.Dekoster,
D.P.Cistola,
and
W.E.Goldman
(2009).
NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B.
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Mol Microbiol,
72,
344-353.
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PDB code:
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L.A.Martin-Visscher,
M.J.van Belkum,
S.Garneau-Tsodikova,
R.M.Whittal,
J.Zheng,
L.M.McMullen,
and
J.C.Vederas
(2008).
Isolation and characterization of carnocyclin a, a novel circular bacteriocin produced by Carnobacterium maltaromaticum UAL307.
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Appl Environ Microbiol,
74,
4756-4763.
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M.Rossmann,
R.Schultz-Heienbrok,
J.Behlke,
N.Remmel,
C.Alings,
K.Sandhoff,
W.Saenger,
and
T.Maier
(2008).
Crystal structures of human saposins C andD: implications for lipid recognition and membrane interactions.
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Structure,
16,
809-817.
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PDB codes:
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C.M.Franz,
M.J.van Belkum,
W.H.Holzapfel,
H.Abriouel,
and
A.Gálvez
(2007).
Diversity of enterococcal bacteriocins and their grouping in a new classification scheme.
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FEMS Microbiol Rev,
31,
293-310.
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W.Theppangna,
T.Murase,
N.Tokumaru,
H.Chikumi,
E.Shimizu,
and
K.Otsuki
(2007).
Screening of the enterocin genes and antimicrobial activity against pathogenic bacteria in Enterococcus strains obtained from different origins.
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J Vet Med Sci,
69,
1235-1239.
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V.E.Ahn,
P.Leyko,
J.R.Alattia,
L.Chen,
and
G.G.Privé
(2006).
Crystal structures of saposins A and C.
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Protein Sci,
15,
1849-1857.
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PDB codes:
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K.Ginalski,
N.V.Grishin,
A.Godzik,
and
L.Rychlewski
(2005).
Practical lessons from protein structure prediction.
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Nucleic Acids Res,
33,
1874-1891.
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C.Folli,
I.Ramazzina,
P.Arcidiaco,
M.Stoppini,
and
R.Berni
(2003).
Purification of bacteriocin AS-48 from an Enterococcus faecium strain and analysis of the gene cluster involved in its production.
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FEMS Microbiol Lett,
221,
143-149.
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C.González,
J.L.Neira,
S.Ventura,
S.Bronsoms,
M.Rico,
and
F.X.Avilés
(2003).
Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR.
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Proteins,
50,
410-422.
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PDB code:
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D.J.Craik,
N.L.Daly,
I.Saska,
M.Trabi,
and
K.J.Rosengren
(2003).
Structures of naturally occurring circular proteins from bacteria.
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J Bacteriol,
185,
4011-4021.
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E.de Alba,
S.Weiler,
and
N.Tjandra
(2003).
Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles.
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Biochemistry,
42,
14729-14740.
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PDB code:
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J.Tsai,
R.Bonneau,
A.V.Morozov,
B.Kuhlman,
C.A.Rohl,
and
D.Baker
(2003).
An improved protein decoy set for testing energy functions for protein structure prediction.
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Proteins,
53,
76-87.
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K.J.Walters,
P.J.Lech,
A.M.Goh,
Q.Wang,
and
P.M.Howley
(2003).
DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a.
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Proc Natl Acad Sci U S A,
100,
12694-12699.
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PDB codes:
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M.Diaz,
E.Valdivia,
M.Martínez-Bueno,
M.Fernández,
A.S.Soler-González,
H.Ramírez-Rodrigo,
and
M.Maqueda
(2003).
Characterization of a new operon, as-48EFGH, from the as-48 gene cluster involved in immunity to enterocin AS-48.
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Appl Environ Microbiol,
69,
1229-1236.
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R.Kemperman,
A.Kuipers,
H.Karsens,
A.Nauta,
O.Kuipers,
and
J.Kok
(2003).
Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574.
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Appl Environ Microbiol,
69,
1589-1597.
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R.Kemperman,
M.Jonker,
A.Nauta,
O.P.Kuipers,
and
J.Kok
(2003).
Functional analysis of the gene cluster involved in production of the bacteriocin circularin A by Clostridium beijerinckii ATCC 25752.
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Appl Environ Microbiol,
69,
5839-5848.
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V.E.Ahn,
K.F.Faull,
J.P.Whitelegge,
A.L.Fluharty,
and
G.G.Privé
(2003).
Crystal structure of saposin B reveals a dimeric shell for lipid binding.
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Proc Natl Acad Sci U S A,
100,
38-43.
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PDB code:
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A.Hofmann,
H.Iwai,
S.Hess,
A.Plückthun,
and
A.Wlodawer
(2002).
Structure of cyclized green fluorescent protein.
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Acta Crystallogr D Biol Crystallogr,
58,
1400-1406.
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PDB code:
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H.Abriouel,
M.Maqueda,
A.Gálvez,
M.Martínez-Bueno,
and
E.Valdivia
(2002).
Inhibition of bacterial growth, enterotoxin production, and spore outgrowth in strains of Bacillus cereus by bacteriocin AS-48.
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Appl Environ Microbiol,
68,
1473-1477.
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M.Trabi,
and
D.J.Craik
(2002).
Circular proteins--no end in sight.
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Trends Biochem Sci,
27,
132-138.
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A.Blond,
M.Cheminant,
I.Ségalas-Milazzo,
J.Péduzzi,
M.Barthélémy,
C.Goulard,
R.Salomón,
F.Moreno,
R.Farías,
and
S.Rebuffat
(2001).
Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli.
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Eur J Biochem,
268,
2124-2133.
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PDB code:
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A.G.Murzin,
and
A.Bateman
(2001).
CASP2 knowledge-based approach to distant homology recognition and fold prediction in CASP4.
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Proteins,
(),
76-85.
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D.T.Jones
(2001).
Predicting novel protein folds by using FRAGFOLD.
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Proteins,
(),
127-132.
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J.Pillardy,
C.Czaplewski,
A.Liwo,
J.Lee,
D.R.Ripoll,
R.Kaźmierkiewicz,
S.Oldziej,
W.J.Wedemeyer,
K.D.Gibson,
Y.A.Arnautova,
J.Saunders,
Y.J.Ye,
and
H.A.Scheraga
(2001).
Recent improvements in prediction of protein structure by global optimization of a potential energy function.
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Proc Natl Acad Sci U S A,
98,
2329-2333.
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R.Bonneau,
J.Tsai,
I.Ruczinski,
D.Chivian,
C.Rohl,
C.E.Strauss,
and
D.Baker
(2001).
Rosetta in CASP4: progress in ab initio protein structure prediction.
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Proteins,
(),
119-126.
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R.del Campo,
C.Tenorio,
R.Jiménez-Díaz,
C.Rubio,
R.Gómez-Lus,
F.Baquero,
and
C.Torres
(2001).
Bacteriocin production in vancomycin-resistant and vancomycin-susceptible Enterococcus isolates of different origins.
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Antimicrob Agents Chemother,
45,
905-912.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
