 |
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
1pzw
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Cellular component
|
nucleus
|
1 term
|
 |
|
Biochemical function
|
zinc ion binding
|
1 term
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Structure
11:1393-1402
(2003)
|
|
PubMed id:
|
|
|
|
|
| |
|
The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module.
|
|
R.Jauch,
G.P.Bourenkov,
H.R.Chung,
H.Urlaub,
U.Reidt,
H.Jäckle,
M.C.Wahl.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
About one-third of the more than 300 C2H2 zinc finger proteins of Drosophila
contain a conserved sequence motif, the zinc finger-associated domain (ZAD).
Genes that encode ZAD proteins are specific for and expanded in the genomes of
insects. Only three ZAD-encoding gene functions are established, and the role of
ZAD is unknown. Here we present the crystal structure of the ZAD of Grauzone
(ZAD(Grau)), a Drosophila transcription factor that specifically controls the
maternal Cdc20-like APC subunit Cortex. ZAD forms an atypical treble-clef-like
zinc-coordinating fold. Head-to-tail arrangement of two ZAD(Grau) molecules in
the crystals suggests dimer formation, an observation supported by crosslinking
and dynamic light scattering. The results indicate that ZAD provides a novel
protein-protein interaction module that characterizes a large family of insect
transcription factors.
|
|
|
|
|
| |
Selected figure(s)
|
|
|
| |
 |
 |
|
 |
Figure 4.
Figure 4. The ZAD[Grau] Dimer(A) Stereo ribbon plot of a
ZAD[Grau] dimer as seen in the crystal. The two subunits (Mol I
and Mol II) are colored red and blue; the two zinc centers are
depicted in ball-and-stick. N- and C termini are labeled. The
orientation of the rear subunit is the same as in Figure 2A.(B)
Stereo representation of residue interactions in the dimer
interface, 90° from the view in (A). The two ZAD[Grau] subunits
are colored as in (A) but are rendered semitransparent to
clearly reveal the interacting residues in ball-and-stick. All
residues and the molecular termini are labeled.(C) Mapping of
the contact residues within the dimer (green) onto the surface
of a ZAD[Grau] monomer (gray). The orientation of the molecule
is the same as that of the red subunit in (A).(D) Mapping in
orange of conserved residues on the surface of ZAD[Grau] in two
diametric views. The left orientation is the same as in (C),
indicating that the largest conserved surface patch and the
dimer interface largely coincide.
|
 |
|
|
|
| |
The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
1393-1402)
copyright 2003.
|
|
| |
Figure was
selected
by an automated process.
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
J.P.Lewandowski,
K.B.Sheehan,
P.E.Bennett,
and
R.E.Boswell
(2010).
Mago Nashi, Tsunagi/Y14, and Ranshi form a complex that influences oocyte differentiation in Drosophila melanogaster.
|
| |
Dev Biol, 339,
307-319.
|
 |
|
|
|
|
 |
L.Aravind,
V.Anantharaman,
and
T.M.Venancio
(2009).
Apprehending multicellularity: regulatory networks, genomics, and evolutiony.
|
| |
Birth Defects Res C Embryo Today, 87,
143-164.
|
 |
|
|
|
|
 |
D.Bessière,
C.Lacroix,
S.Campagne,
V.Ecochard,
V.Guillet,
L.Mourey,
F.Lopez,
J.Czaplicki,
P.Demange,
A.Milon,
J.P.Girard,
and
V.Gervais
(2008).
Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways.
|
| |
J Biol Chem, 283,
4352-4363.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
R.Jauch,
S.Jäkel,
C.Netter,
K.Schreiter,
B.Aicher,
H.Jäckle,
and
M.C.Wahl
(2005).
Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site.
|
| |
Structure, 13,
1559-1568.
|
 |
|
PDB codes:
|
 |
|
|
 |
 |
|
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.
|
|