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PDBsum entry 1abh
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Phosphotransferase
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PDB id
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1abh
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References listed in PDB file
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Key reference
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Title
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High specificity of a phosphate transport protein determined by hydrogen bonds.
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Authors
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H.Luecke,
F.A.Quiocho.
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Ref.
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Nature, 1990,
347,
402-406.
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PubMed id
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Abstract
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Transport of the essential nutrient phosphorus--primarily in the form of
orthophosphate--into cells and organelles is highly specific. This is
exemplified by the uptake of phosphate or its close analogue arsenate by
bacterial cells by way of a high affinity active transport system dependent on a
phosphate-binding protein; this system is unable to recognize other inorganic
oxyanions and is, moreover, distinct from the one for sulphate transport. The
phosphate-binding protein is a member of a family of periplasmic proteins acting
as initial high-affinity receptors for the osmotic shock-sensitive active
transport systems or permeases for various sugars, amino acids, oligopeptides,
and oxyanions. We report here the highly refined 1.7 A resolution X-ray
structure of the liganded form of the phosphate-binding protein. The structure
reveals the atomic features responsible for phosphate selectivity, either in
monobasic or dibasic form, and the exclusion of sulphate. These features are
fundamental to understanding phosphate transport systems and molecular
recognition of charged substrates or ions in other biological processes.
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Secondary reference #1
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Title
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Crystallization and X-Ray diffraction studies of a phosphate-Binding protein involved in active transport in escherichia coli.
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Authors
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B.D.Kubena,
H.Luecke,
H.Rosenberg,
F.A.Quiocho.
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Ref.
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J Biol Chem, 1986,
261,
7995-7996.
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PubMed id
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Secondary reference #2
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Title
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Structural gene for the phosphate-Repressible phosphate-Binding protein of escherichia coli has its own promoter: complete nucleotide sequence of the phos gene.
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Authors
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B.P.Surin,
D.A.Jans,
A.L.Fimmel,
D.C.Shaw,
G.B.Cox,
H.Rosenberg.
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Ref.
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J Bacteriol, 1984,
157,
772-778.
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PubMed id
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