 |
PDBsum entry 1cw6
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Toxin
|
|
|
Title:
|
|
Refined solution structure of leucocin a
|
|
Structure:
|
|
Type iia bacteriocin leucocin a. Chain: a. Fragment: leucocin a-ual 187
|
|
Source:
|
|
Leuconostoc gelidum. Organism_taxid: 1244
|
|
NMR struc:
|
|
18 models
|
|
|
Authors:
|
|
Y.Wang,M.E.Henz,N.L.F.Gallagher,S.Chai,L.Z.Yan,A.C.Gibbs,M.E.Stiles, D.S.Wishart,J.C.Vederas
|
Key ref:
|
|
Y.Wang
et al.
(1999).
Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria.
Biochemistry,
38,
15438-15447.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
25-Aug-99
|
Release date:
|
08-Sep-99
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P34034
(LCCA_LEUGE) -
Bacteriocin leucocin-A from Leuconostoc gelidum
|
|
|
|
Seq:
Struc:
|
|
|
|
61 a.a.
37 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Biochemistry
38:15438-15447
(1999)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria.
|
|
Y.Wang,
M.E.Henz,
N.L.Gallagher,
S.Chai,
A.C.Gibbs,
L.Z.Yan,
M.E.Stiles,
D.S.Wishart,
J.C.Vederas.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Carnobacteriocin B2 (CbnB2), a type IIa bacteriocin, is a 48 residue
antimicrobial peptide from the lactic acid bacterium Carnobacterium pisicola
LV17B. Type IIa bacteriocins have a conserved YGNGVXC sequence near the
N-terminus and usually contain a disulfide bridge. CbnB2 seemed to be unique in
that its two cysteines (Cys9 and Cys14) could be isolated as free thiols [Quadri
et al. (1994) J. Biol. Chem. 26, 12204-12211]. To establish the structural
consequences of the presence or absence of a disulfide bridge and to investigate
if the YGNGVXC sequence is a receptor-binding motif [Fleury et al. (1996) J.
Biol. Chem. 271, 14421-14429], the three-dimensional solution structure of CbnB2
was determined by two-dimensional (1)H nuclear magnetic resonance (NMR)
techniques. Mass spectroscopic and thiol modification experiments on CbnB2 and
on model peptides, in conjunction with activity measurements, were used to
verify the redox status of CbnB2. The results show that CbnB2 readily forms a
disulfide bond and that this peptide has full antimicrobial activity. NMR
results indicate that CbnB2 in trifluoroethanol (TFE) has a well-defined central
helical structure (residues 18-39) but a disordered N terminus. Comparison of
the CbnB2 structure with the refined solution structure of leucocin A (LeuA),
another type IIa bacteriocin, indicates that the central helical structure is
conserved between the two peptides despite differences in sequence but that the
N-terminal structure (a proposed receptor binding site) is not. This is
unexpected because LeuA and CbnB2 exhibit >66% sequence identity in the first
24 residues. This suggests that the N-terminus, which had been proposed [Fleury
et al. (1996) J. Biol. Chem. 271, 14421-14429] to be a receptor binding site of
type IIa bacteriocins, may not be directly involved and that recognition of the
amphiphilic helical portion is the critical feature.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
E.C.Hobbs,
F.Fontaine,
X.Yin,
and
G.Storz
(2011).
An expanding universe of small proteins.
|
| |
Curr Opin Microbiol,
14,
167-173.
|
|
|
|
|
|
|
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.
|
| |
Protein Eng Des Sel,
23,
507-518.
|
|
|
|
|
|
|
J.Nissen-Meyer,
C.Oppegård,
P.Rogne,
H.S.Haugen,
and
P.E.Kristiansen
(2010).
Structure and Mode-of-Action of the Two-Peptide (Class-IIb) Bacteriocins.
|
| |
Probiotics Antimicrob Proteins,
2,
52-60.
|
|
|
|
|
|
|
G.Feng,
G.K.Guron,
J.J.Churey,
and
R.W.Worobo
(2009).
Characterization of mundticin L, a class IIa anti-Listeria bacteriocin from Enterococcus mundtii CUGF08.
|
| |
Appl Environ Microbiol,
75,
5708-5713.
|
|
|
|
|
|
|
J.Rihakova,
V.W.Petit,
K.Demnerova,
H.Prévost,
S.Rebuffat,
and
D.Drider
(2009).
Insights into structure-activity relationships in the C-terminal region of divercin V41, a class IIa bacteriocin with high-level antilisterial activity.
|
| |
Appl Environ Microbiol,
75,
1811-1819.
|
|
|
|
|
|
|
C.S.Sit,
and
J.C.Vederas
(2008).
Approaches to the discovery of new antibacterial agents based on bacteriocins.
|
| |
Biochem Cell Biol,
86,
116-123.
|
|
|
|
|
|
|
D.J.Derksen,
M.A.Boudreau,
and
J.C.Vederas
(2008).
Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1.
|
| |
Chembiochem,
9,
1898-1901.
|
|
|
|
|
|
|
H.S.Haugen,
P.E.Kristiansen,
G.Fimland,
and
J.Nissen-Meyer
(2008).
Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes.
|
| |
Appl Environ Microbiol,
74,
6766-6773.
|
|
|
|
|
|
|
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.
|
| |
Appl Environ Microbiol,
74,
4756-4763.
|
|
|
|
|
|
|
I.K.Kim,
M.K.Kim,
J.H.Kim,
H.S.Yim,
S.S.Cha,
and
S.O.Kang
(2007).
High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins.
|
| |
BMC Struct Biol,
7,
35.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
J.J.Leisner,
B.G.Laursen,
H.Prévost,
D.Drider,
and
P.Dalgaard
(2007).
Carnobacterium: positive and negative effects in the environment and in foods.
|
| |
FEMS Microbiol Rev,
31,
592-613.
|
|
|
|
|
|
|
T.Tominaga,
and
Y.Hatakeyama
(2007).
Development of innovative pediocin PA-1 by DNA shuffling among class IIa bacteriocins.
|
| |
Appl Environ Microbiol,
73,
5292-5299.
|
|
|
|
|
|
|
C.Landon,
H.Meudal,
N.Boulanger,
P.Bulet,
and
F.Vovelle
(2006).
Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.
|
| |
Biopolymers,
81,
92.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
D.Drider,
G.Fimland,
Y.Héchard,
L.M.McMullen,
and
H.Prévost
(2006).
The continuing story of class IIa bacteriocins.
|
| |
Microbiol Mol Biol Rev,
70,
564-582.
|
|
|
|
|
|
|
T.Tominaga,
and
Y.Hatakeyama
(2006).
Determination of essential and variable residues in pediocin PA-1 by NNK scanning.
|
| |
Appl Environ Microbiol,
72,
1141-1147.
|
|
|
|
|
|
|
L.Johnsen,
B.Dalhus,
I.Leiros,
and
J.Nissen-Meyer
(2005).
1.6-Angstroms crystal structure of EntA-im. A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A.
|
| |
J Biol Chem,
280,
19045-19050.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
L.Johnsen,
G.Fimland,
and
J.Nissen-Meyer
(2005).
The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum.
|
| |
J Biol Chem,
280,
9243-9250.
|
|
|
|
|
|
|
D.Morisset,
J.M.Berjeaud,
D.Marion,
C.Lacombe,
and
J.Frère
(2004).
Mutational analysis of mesentericin y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction.
|
| |
Appl Environ Microbiol,
70,
4672-4680.
|
|
|
|
|
|
|
G.M.Gibbs,
B.E.Davidson,
and
A.J.Hillier
(2004).
Novel expression system for large-scale production and purification of recombinant class IIa bacteriocins and its application to piscicolin 126.
|
| |
Appl Environ Microbiol,
70,
3292-3297.
|
|
|
|
|
|
|
I.F.Nes,
and
O.Johnsborg
(2004).
Exploration of antimicrobial potential in LAB by genomics.
|
| |
Curr Opin Biotechnol,
15,
100-104.
|
|
|
|
|
|
|
L.Johnsen,
G.Fimland,
D.Mantzilas,
and
J.Nissen-Meyer
(2004).
Structure-function analysis of immunity proteins of pediocin-like bacteriocins: C-terminal parts of immunity proteins are involved in specific recognition of cognate bacteriocins.
|
| |
Appl Environ Microbiol,
70,
2647-2652.
|
|
|
|
|
|
|
T.Sprules,
K.E.Kawulka,
A.C.Gibbs,
D.S.Wishart,
and
J.C.Vederas
(2004).
NMR solution structure of the precursor for carnobacteriocin B2, an antimicrobial peptide from Carnobacterium piscicola.
|
| |
Eur J Biochem,
271,
1748-1756.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
B.Dalhus,
L.Johnsen,
and
J.Nissen-Meyer
(2003).
Crystallization and preliminary X-ray data investigation of the bacterial enterocin A immunity protein at 1.65 A resolution.
|
| |
Acta Crystallogr D Biol Crystallogr,
59,
1291-1293.
|
|
|
|
|
|
|
N.I.Martin,
H.Hu,
M.M.Moake,
J.J.Churey,
R.Whittal,
R.W.Worobo,
and
J.C.Vederas
(2003).
Isolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M.
|
| |
J Biol Chem,
278,
13124-13132.
|
|
|
|
|
|
|
S.Garneau,
C.A.Ference,
M.J.van Belkum,
M.E.Stiles,
and
J.C.Vederas
(2003).
Purification and characterization of brochocin A and brochocin B(10-43), a functional fragment generated by heterologous expression in Carnobacterium piscicola.
|
| |
Appl Environ Microbiol,
69,
1352-1358.
|
|
|
|
|
|
|
M.Uteng,
H.H.Hauge,
I.Brondz,
J.Nissen-Meyer,
and
G.Fimland
(2002).
Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium.
|
| |
Appl Environ Microbiol,
68,
952-956.
|
|
|
|
|
|
|
M.Ferchichi,
J.Frère,
K.Mabrouk,
and
M.Manai
(2001).
Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product.
|
| |
FEMS Microbiol Lett,
205,
49-55.
|
|
|
|
|
|
|
G.Fimland,
L.Johnsen,
L.Axelsson,
M.B.Brurberg,
I.F.Nes,
V.G.Eijsink,
and
J.Nissen-Meyer
(2000).
A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum.
|
| |
J Bacteriol,
182,
2643-2648.
|
|
|
|
|
|
|
I.F.Nes,
and
H.Holo
(2000).
Class II antimicrobial peptides from lactic acid bacteria.
|
| |
Biopolymers,
55,
50-61.
|
|
|
|
|
|
|
L.Johnsen,
G.Fimland,
V.Eijsink,
and
J.Nissen-Meyer
(2000).
Engineering increased stability in the antimicrobial peptide pediocin PA-1.
|
| |
Appl Environ Microbiol,
66,
4798-4802.
|
|
|
|
|
|
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.
|
|
Links
