 |
PDBsum entry 1ed0
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Biochem J
350:569-577
(2000)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
NMR structural determination of viscotoxin A3 from Viscum album L.
|
|
S.Romagnoli,
R.Ugolini,
F.Fogolari,
G.Schaller,
K.Urech,
M.Giannattasio,
L.Ragona,
H.Molinari.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The high-resolution three-dimensional structure of the plant toxin viscotoxin
A3, from Viscum album L., has been determined in solution by (1)H NMR
spectroscopy at pH 3.6 and 12 degrees C (the structure has been deposited in the
Protein Data Bank under the id. code 1ED0). Experimentally derived restraints
including 734 interproton distances from nuclear Overhauser effect measurements,
22 hydrogen bonds, 32 φ angle restraints from J coupling measurements,
together with three disulphide bridge constraints were used as input in
restrained molecular dynamics, followed by minimization, using DYANA and
Discover. Backbone and heavy atom root-mean-square deviations were 0.47+/-0.11 A
(1 A=10(-10) m) and 0.85+/-0.13 A respectively. Viscotoxin A3 consists of two
alpha-helices connected by a turn and a short stretch of antiparallel
beta-sheet. This fold is similar to that found in other thionins, such as
crambin, hordothionin-alpha and -beta, phoratoxin A and purothionin-alpha and
-beta. The difference in the observed biological activity for thionins of known
structure is discussed in terms of the differences in the calculated surface
potential distribution, playing an important role in their function through
disruption of cell membranes. In addition, the possible role in DNA binding of
the helix-turn-helix motif of viscotoxin A3 is discussed.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
Y.Cote,
P.Senet,
P.Delarue,
G.G.Maisuradze,
and
H.A.Scheraga
(2010).
Nonexponential decay of internal rotational correlation functions of native proteins and self-similar structural fluctuations.
|
| |
Proc Natl Acad Sci U S A,
107,
19844-19849.
|
|
|
|
|
|
|
A.Pal,
J.E.Debreczeni,
M.Sevvana,
T.Gruene,
B.Kahle,
A.Zeeck,
and
G.M.Sheldrick
(2008).
Structures of viscotoxins A1 and B2 from European mistletoe solved using native data alone.
|
| |
Acta Crystallogr D Biol Crystallogr,
64,
985-992.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
M.Giudici,
J.A.Poveda,
M.L.Molina,
L.de la Canal,
J.M.González-Ros,
K.Pfüller,
U.Pfüller,
and
J.Villalaín
(2006).
Antifungal effects and mechanism of action of viscotoxin A3.
|
| |
FEBS J,
273,
72-83.
|
|
|
|
|
|
|
F.Fogolari,
A.Brigo,
and
H.Molinari
(2003).
Protocol for MM/PBSA molecular dynamics simulations of proteins.
|
| |
Biophys J,
85,
159-166.
|
|
|
|
|
|
|
M.Giudici,
R.Pascual,
L.de la Canal,
K.Pfüller,
U.Pfüller,
and
J.Villalaín
(2003).
Interaction of viscotoxins A3 and B with membrane model systems: implications to their mechanism of action.
|
| |
Biophys J,
85,
971-981.
|
|
|
|
|
|
|
F.Fogolari,
A.Brigo,
and
H.Molinari
(2002).
The Poisson-Boltzmann equation for biomolecular electrostatics: a tool for structural biology.
|
| |
J Mol Recognit,
15,
377-392.
|
|
|
|
|
|
|
F.Fogolari,
G.Esposito,
P.Viglino,
and
H.Molinari
(2001).
Molecular mechanics and dynamics of biomolecules using a solvent continuum model.
|
| |
J Comput Chem,
22,
1830-1842.
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
