 |
PDBsum entry 9abp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Binding proteins
|
PDB id
|
|
|
|
9abp
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
A pro to gly mutation in the hinge of the arabinose-Binding protein enhances binding and alters specificity. Sugar-Binding and crystallographic studies.
|
|
|
Authors
|
|
P.S.Vermersch,
J.J.Tesmer,
D.D.Lemon,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1990,
265,
16592-16603.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The L-arabinose-binding protein (ABP) of Escherichia coli consists structurally
of two distinct globular domains connected by a hinge of three separate peptide
segments. Arabinose is bound and completely sequestered within the deep cleft
between the two domains. With reduced affinity, ABP also binds D-galactose
(approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
Experiments have been conducted to explore the role in sugar binding of the
hinge connecting the two domains of ABP. To increase the flexibility of the
hinge region, a glycine was substituted for a proline at position 254 by
site-directed mutagenesis. Unexpectedly, this mutation resulted in the dramatic
enhancement of galactose binding over that of arabinose. The affinity of the
mutant ABP for galactose increased by over 20-fold, while that for arabinose and
fucose remained relatively unchanged. We have measured association and
dissociation rates of the Gly-254 ABP with L-arabinose, D-galactose, and
D-fucose and have determined the crystallographic structure of the protein
complexed with each of the three sugars. Both the ligand-binding kinetic
measurements and structure analysis indicate that the altered specificity is due
to an effective increase in the rigidity of the hinge in the closed conformation
which is induced upon galactose binding. Stabilizing contacts are formed between
the strands of the hinge in the Gly-254 ABP when galactose is bound which are
not found in complexes with the other sugars or the liganded wild-type protein.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Substrate specificity and affinity of a protein modulated by bound water molecules.
|
|
|
Authors
|
|
F.A.Quiocho,
D.K.Wilson,
N.K.Vyas.
|
|
|
Ref.
|
|
Nature, 1989,
340,
404-407.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Novel stereospecificity of the l-Arabinose-Binding protein.
|
|
|
Authors
|
|
F.A.Quiocho,
N.K.Vyas.
|
|
|
Ref.
|
|
Nature, 1984,
310,
381-386.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Hinge-Bending in l-Arabinose-Binding protein. The "venus'S-Flytrap" model.
|
|
|
Authors
|
|
B.Mao,
M.R.Pear,
J.A.Mccammon,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1982,
257,
1131-1133.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #4
|
|
|
Title
|
|
Structure of the l-Arabinose-Binding protein from escherichia coli at 2.4 a resolution.
|
|
|
Authors
|
|
G.L.Gilliland,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Mol Biol, 1981,
146,
341-362.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 3.
FVG
G VI H
H VII I
I VIII
J - L/l
|
|
Figure 6.
Fro. 6. A stereo view showing the location of acidic and basic residues. An iarabinose model
representing both anomers is in the cleft. The positively charged residues Lys, Arg and His, and te
negatively charged residues Glu and Asp are highlighted by thicker lines.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
with permission from Elsevier
|
|
|
Secondary reference #5
|
|
|
Title
|
|
L-Arabinose-Binding protein-Sugar complex at 2.4 a resolution. Stereochemistry and evidence for a structural change.
|
|
|
Authors
|
|
M.E.Newcomer,
G.L.Gilliland,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1981,
256,
13213-13217.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #6
|
|
|
Title
|
|
The radius of gyration of l-Arabinose-Binding protein decreases upon binding of ligand.
|
|
|
Authors
|
|
M.E.Newcomer,
B.A.Lewis,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1981,
256,
13218-13222.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #7
|
|
|
Title
|
|
The thiol group of the l-Arabinose-Binding protein. Chromophoric labeling and chemical identification of the sugar-Binding site.
|
|
|
Authors
|
|
D.M.Miller,
M.E.Newcomer,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1979,
254,
7521-7528.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #8
|
|
|
Title
|
|
Location of the sugar-Binding site of l-Arabinose-Binding protein. Sugar derivative syntheses, Sugar binding specificity, And difference fourier analyses.
|
|
|
Authors
|
|
M.E.Newcomer,
D.M.Miller,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1979,
254,
7529-7533.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #9
|
|
|
Title
|
|
The 2.8-A resolution structure of the l-Arabinose-Binding protein from escherichia coli. Polypeptide chain folding, Domain similarity, And probable location of sugar-Binding site.
|
|
|
Authors
|
|
F.A.Quiocho,
G.L.Gilliland,
G.N.Phillips.
|
|
|
Ref.
|
|
J Biol Chem, 1977,
252,
5142-5149.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #10
|
|
|
Title
|
|
Structure of l-Arabinose-Binding protein from escherichia coli at 5 a resolution and preliminary results at 3.5 a.
|
|
|
Authors
|
|
G.N.Phillips,
V.K.Mahajan,
A.K.Siu,
F.A.Quiocho.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 1976,
73,
2186-2190.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
