 |
PDBsum entry 1prv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
1prv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural comparison of the free and DNA-Bound forms of the purine repressor DNA-Binding domain.
|
|
|
Authors
|
|
A.Nagadoi,
S.Morikawa,
H.Nakamura,
M.Enari,
K.Kobayashi,
H.Yamamoto,
G.Sampei,
K.Mizobuchi,
M.A.Schumacher,
R.G.Brennan.
|
|
|
Ref.
|
|
Structure, 1995,
3,
1217-1224.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
BACKGROUND: The purine repressor (PurR) regulates genes that encode enzymes for
purine biosynthesis. PurR has a two domain structure with an N-terminal
DNA-binding domain (DBD) and a C-terminal corepressor-binding domain (CBD). The
three dimensional structure of a ternary complex of PurR bound to both
corepressor and a specific DNA sequence has recently been determined by X-ray
crystallography. RESULTS: We have determined the solution structure of the PurR
DBD by NMR. It contains three helices, with the first and second helices forming
a helix-turn-helix motif. The tertiary structure of the three helices is very
similar to that of the corresponding region in the ternary complex. The
structure of the hinge helical region, however, which makes specific base
contacts in the minor groove of DNA, is disordered in the DNA-free form.
CONCLUSION: The stable formation of PurR hinge helices requires PurR
dimerization, which brings the hinge regions proximal to each other. The
dimerization of the hinge helices is likely to be controlled by the CBD
dimerization interface, but is induced by specific-DNA binding.
|
|
|
|
|
|
|
|
Figure 3.
Figure 3. Stereoview of the best-fit superpositions of the 20
PurN56 structures, along with the refined average structure.
Met1–Pro47 is shown in yellow for the 20 structures and in red
for the average structure, and Ser48–Val56 is green for the
20 structures. No average structure is shown for the C-terminal
residues. Figure 3. Stereoview of the best-fit
superpositions of the 20 PurN56 structures, along with the
refined average structure. Met1–Pro47 is shown in yellow for
the 20 structures and in red for the average structure, and
Ser48–Val56 is green for the 20 structures. No average
structure is shown for the C-terminal residues.
|
|
Figure 7.
Figure 7. A best-fit superposition of the free PurR DBD
structure onto the ternary complex structure of the
PurR–hypoxanthine–purF-operator. The backbone atoms of the
free PurR DBD (Met1–Ser48) are shown in yellow, and the
backbone atoms of PurR dimer in the ternary complex are shown in
blue and red, the two colours distinguishing the two monomers.
The DNA atoms are shown in pink and white. Two hypoxanthine
molecules bound to PurR dimer are also shown in white. Figure
7. A best-fit superposition of the free PurR DBD structure onto
the ternary complex structure of the
PurR–hypoxanthine–purF-operator. The backbone atoms of the
free PurR DBD (Met1–Ser48) are shown in yellow, and the
backbone atoms of PurR dimer in the ternary complex are shown in
blue and red, the two colours distinguishing the two monomers.
The DNA atoms are shown in pink and white. Two hypoxanthine
molecules bound to PurR dimer are also shown in white.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Structure
(1995,
3,
1217-1224)
copyright 1995.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystal structure of laci member, Purr, Bound to DNA: minor groove binding by alpha helices.
|
|
|
Authors
|
|
M.A.Schumacher,
K.Y.Choi,
H.Zalkin,
R.G.Brennan.
|
|
|
Ref.
|
|
Science, 1994,
266,
763-770.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
