 |
PDBsum entry 1glg
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Galactose-binding protein
|
PDB id
|
|
|
|
1glg
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for d-Glucose and d-Galactose.
|
|
|
Authors
|
|
M.N.Vyas,
N.K.Vyas,
F.A.Quiocho.
|
|
|
Ref.
|
|
Biochemistry, 1994,
33,
4762-4768.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The D-glucose/D-galactose-binding protein (M(r) = 33,000) found in the periplasm
of bacterial cells serves as the primary high-affinity receptor of active
transport for and chemotaxis toward both sugar epimers. This protein from
Escherichia coli binds D-glucose with a Kd of 2 x 10(-7) M, which is about 2
times tighter than D-galactose. The 2.0-A resolution crystal structure of the
binding protein complexed with D-galactose has been refined to a
crystallographic R-factor of 0.167. This structure, combined with that
previously refined for the complex with D-glucose [Vyas, N.K., Vyas., M. N.,
& Quiocho, F. A. (1988) Science 242, 1290-1295], provides understanding, in
atomic detail, of recognition of sugar epimers and anomers. In the two complex
structures, the sugar ring is positioned identically in the binding site, and
each hydroxyl group common to both is involved in very similar cooperative
hydrogen-bonding interactions with protein residues and ordered water molecules.
Only the beta-anomer of both monosaccharides is bound, with Asp154 OD1 primarily
responsible for accepting a hydrogen bond from the anomeric hydroxyl.
Recognition of both sugar epimers is accomplished principally by hydrogen
bonding of Asp14 OD1 with the equatorial OH4 of D-glucose and OD2 with the axial
OH4 of D-galactose. These results are reconciled with equilibrium and fast
kinetics data, which indicate binding of both anomers of the two sugars, and
further compared with sugar recognition by other periplasmic sugar-binding
proteins with specificities for arabinose/galactose/fucose,
maltooligosaccharides, and ribose.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Comparison of the periplasmic receptors for l-Arabinose, D-Glucose/d-Galactose, And d-Ribose. Structural and functional similarity.
|
|
|
Authors
|
|
N.K.Vyas,
M.N.Vyas,
F.A.Quiocho.
|
|
|
Ref.
|
|
J Biol Chem, 1991,
266,
5226-5237.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Sugar and signal-Transducer binding sites of the escherichia coli galactose chemoreceptor protein.
|
|
|
Authors
|
|
N.K.Vyas,
M.N.Vyas,
F.A.Quiocho.
|
|
|
Ref.
|
|
Science, 1988,
242,
1290-1295.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
A novel calcium binding site in the galactose-Binding protein of bacterial transport and chemotaxis.
|
|
|
Authors
|
|
N.K.Vyas,
M.N.Vyas,
F.A.Quiocho.
|
|
|
Ref.
|
|
Nature, 1987,
327,
635-638.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
