|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
96 a.a.
|
|
|
|
|
|
|
|
|
|
|
96 a.a.
|
|
|
|
|
|
|
|
|
|
|
95 a.a.
|
|
|
|
|
|
|
|
|
|
|
100 a.a.
|
|
|
|
|
|
|
|
|
|
|
93 a.a.
|
|
|
|
|
|
|
|
|
|
|
102 a.a.
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Toxin
|
|
|
Title:
|
|
Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9a crystal structure reveals the details
|
|
Structure:
|
|
Cholera enterotoxin subunit b, heat-labile enterotoxin b chain. Chain: d, e, f, g, h, i, j, k, l, m. Engineered: yes
|
|
Source:
|
|
Vibrio cholerae. Organism_taxid: 666. Strain: js1569. Expressed in: vibrio cholerae. Expression_system_taxid: 666.
|
|
Resolution:
|
|
|
1.94Å
|
R-factor:
|
0.184
|
R-free:
|
0.232
|
|
|
Authors:
|
|
A.Holmner,M.Lebens,S.Teneberg,J.Angstrom,M.Okvist,U.Krengel
|
Key ref:
|
|
A.Holmner
et al.
(2004).
Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.
Structure,
12,
1655-1667.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
10-Sep-08
|
Release date:
|
23-Sep-08
|
|
|
Supersedes:
|
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P01556
(CHTB_VIBCH) -
Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
96 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P0CK94
(ELBH_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
96 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P01556
(CHTB_VIBCH) -
Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
96 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P0CK94
(ELBH_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
96 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P01556
(CHTB_VIBCH) -
Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
95 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P0CK94
(ELBH_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
95 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P01556
(CHTB_VIBCH) -
Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
100 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P0CK94
(ELBH_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
100 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P01556
(CHTB_VIBCH) -
Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
93 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P0CK94
(ELBH_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
|
|
|
|
Seq:
Struc:
|
|
|
|
124 a.a.
93 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Structure
12:1655-1667
(2004)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.
|
|
A.Holmner,
M.Lebens,
S.Teneberg,
J.Angström,
M.Okvist,
U.Krengel.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
A hybrid between the B subunits of cholera toxin and Escherichia coli
heat-labile enterotoxin has been described, which exhibits a novel binding
specificity to blood group A and B type 2 determinants. In the present
investigation, we have determined the crystal structure of this protein hybrid,
termed LCTBK, in complex with the blood group A pentasaccharide
GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the
novel binding specificity but also a distinct new oligosaccharide binding site.
Binding studies revealed that the new specificity can be ascribed to a single
mutation (S4N) introduced into the sequence of Escherichia coli heat-labile
enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in
excellent detail. Main features include a complex network of water molecules,
which is well preserved by the parent toxins, and an unexpectedly modest
contribution to binding by the critical residue Asn4, which interacts with the
ligand only via a single water molecule.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
Figure 4.
Figure 4. View of the Novel Binding Site in a Shallow
Groove at the Interface of Two B Subunits of LCTBK(A) Overview
picture. The blood group A pentasaccharide is shown in stick
representation; the GM1 pentasaccharide is indicated by white
spheres. (Inset: positions of the novel binding site and the GM1
binding site within the B-pentamer, marked with red and white
circles, respectively). Please note that the carbohydrate ligand
is only displayed for one of the five equivalent binding sites
within the B-pentamer.(B) Close-up view of the blood group A
binding site, featuring the two separate water networks (figure
generated with Swiss-PdbViewer and POV-Ray).
|
|
|
|
|
|
| |
The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
1655-1667)
copyright 2004.
|
|
| |
Figure was
selected
by the author.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
D.Das,
P.Kozbial,
G.W.Han,
D.Carlton,
L.Jaroszewski,
P.Abdubek,
T.Astakhova,
H.L.Axelrod,
C.Bakolitsa,
C.Chen,
H.J.Chiu,
M.Chiu,
T.Clayton,
M.C.Deller,
L.Duan,
K.Ellrott,
M.A.Elsliger,
D.Ernst,
C.L.Farr,
J.Feuerhelm,
A.Grzechnik,
J.C.Grant,
K.K.Jin,
H.A.Johnson,
H.E.Klock,
M.W.Knuth,
S.S.Krishna,
A.Kumar,
D.Marciano,
D.McMullan,
M.D.Miller,
A.T.Morse,
E.Nigoghossian,
A.Nopakun,
L.Okach,
S.Oommachen,
J.Paulsen,
C.Puckett,
R.Reyes,
C.L.Rife,
N.Sefcovic,
H.J.Tien,
C.B.Trame,
H.van den Bedem,
D.Weekes,
T.Wooten,
Q.Xu,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
and
I.A.Wilson
(2010).
The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
66,
1254-1260.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
L.Jansson,
J.Angström,
M.Lebens,
and
S.Teneberg
(2010).
No direct binding of the heat-labile enterotoxin of Escherichia coli to E. coli lipopolysaccharides.
|
| |
Glycoconj J,
27,
171-179.
|
|
|
|
|
|
|
B.Mudrak,
D.L.Rodriguez,
and
M.J.Kuehn
(2009).
Residues of heat-labile enterotoxin involved in bacterial cell surface binding.
|
| |
J Bacteriol,
191,
2917-2925.
|
|
|
|
|
|
|
E.M.Galván,
G.A.Roth,
and
C.G.Monferran
(2006).
Functional interaction of Escherichia coli heat-labile enterotoxin with blood group A-active glycoconjugates from differentiated HT29 cells.
|
| |
FEBS J,
273,
3444-3453.
|
|
|
|
|
|
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
