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PDBsum entry 1vmo
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Membrane protein
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PDB id
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1vmo
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Contents |
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* Residue conservation analysis
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Embo J
13:1003-1010
(1994)
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PubMed id:
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Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry.
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T.Shimizu,
D.G.Vassylyev,
S.Kido,
Y.Doi,
K.Morikawa.
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ABSTRACT
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The crystal structure of vitelline membrane outer layer protein I (VMO-I), which
is isolated from the vitelline membrane outer layer of hen's eggs, has been
determined by the multiple isomorphous replacement method and refined to an
R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual
structure that consists of three beta-sheets forming Greek key motifs, which are
related by an internal pseudo three-fold symmetry. The internal portion
surrounded by these three beta-sheets is filled with hydrophobic side chains.
This conformational feature coincides with three internal repeats in the
sequence. Although a similar fold exists in the second domain of
delta-endotoxin, there are significant structural differences between the two
proteins, with the three-fold symmetry being most regular in VMO-I.
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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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H.D.Park,
Y.Lee,
Y.K.Oh,
J.G.Jung,
Y.W.Park,
K.Myung,
K.H.Kim,
S.S.Koh,
and
D.S.Lim
(2011).
Pancreatic adenocarcinoma upregulated factor promotes metastasis by regulating TLR/CXCR4 activation.
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Oncogene,
30,
201-211.
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Z.Chen,
F.A.Shamsi,
K.Li,
Q.Huang,
A.A.Al-Rajhi,
I.A.Chaudhry,
and
K.Wu
(2011).
Comparison of camel tear proteins between summer and winter.
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Mol Vis,
17,
323-331.
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K.Mann
(2008).
Proteomic analysis of the chicken egg vitelline membrane.
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Proteomics,
8,
2322-2332.
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C.R.Pigott,
and
D.J.Ellar
(2007).
Role of receptors in Bacillus thuringiensis crystal toxin activity.
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Microbiol Mol Biol Rev,
71,
255-281.
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T.J.Oldfield
(2007).
CAALIGN: a program for pairwise and multiple protein-structure alignment.
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Acta Crystallogr D Biol Crystallogr,
63,
514-525.
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M.Oobatake,
T.Yamasaki,
J.P.Simmer,
and
V.Renugopalakrishnan
(2006).
Thermal denaturation of a recombinant mouse amelogenin: circular dichroism and differential scanning calorimetric studies.
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Proteins,
62,
461-469.
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K.N.Rao,
C.G.Suresh,
U.V.Katre,
S.M.Gaikwad,
and
M.I.Khan
(2004).
Two orthorhombic crystal structures of a galactose-specific lectin from Artocarpus hirsuta in complex with methyl-alpha-D-galactose.
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Acta Crystallogr D Biol Crystallogr,
60,
1404-1412.
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PDB codes:
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J.C.Rosa,
P.S.De Oliveira,
R.Garratt,
L.Beltramini,
K.Resing,
M.C.Roque-Barreira,
and
L.J.Greene
(1999).
KM+, a mannose-binding lectin from Artocarpus integrifolia: amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the beta-prism fold.
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Protein Sci,
8,
13-24.
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Y.Bourne,
V.Zamboni,
A.Barre,
W.J.Peumans,
E.J.Van Damme,
and
P.Rougé
(1999).
Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins.
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Structure,
7,
1473-1482.
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PDB codes:
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C.Chothia,
T.Hubbard,
S.Brenner,
H.Barns,
and
A.Murzin
(1997).
Protein folds in the all-beta and all-alpha classes.
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Annu Rev Biophys Biomol Struct,
26,
597-627.
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C.S.Wright
(1997).
New folds of plant lectins.
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Curr Opin Struct Biol,
7,
631-636.
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R.Sankaranarayanan,
K.Sekar,
R.Banerjee,
V.Sharma,
A.Surolia,
and
M.Vijayan
(1996).
A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold.
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Nat Struct Biol,
3,
596-603.
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PDB code:
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T.Shimizu,
and
K.Morikawa
(1996).
The beta-prism: a new folding motif.
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Trends Biochem Sci,
21,
3-6.
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Y.Kato,
T.Muto,
T.Tomura,
H.Tsumura,
H.Watarai,
T.Mikayama,
K.Ishizaka,
and
R.Kuroki
(1996).
The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheets.
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Proc Natl Acad Sci U S A,
93,
3007-3010.
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PDB code:
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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
codes are
shown on the right.
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Links
