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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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Nature
347:402-406
(1990)
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PubMed id:
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High specificity of a phosphate transport protein determined by hydrogen bonds.
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H.Luecke,
F.A.Quiocho.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Elias,
A.Wellner,
K.Goldin-Azulay,
E.Chabriere,
J.A.Vorholt,
T.J.Erb,
and
D.S.Tawfik
(2012).
The molecular basis of phosphate discrimination in arsenate-rich environments.
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Nature,
491,
134-137.
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PDB codes:
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C.H.Lee,
H.Yoon,
P.Kim,
S.Cho,
D.Kim,
and
W.D.Jang
(2011).
An indolocarbazole-bridged macrocyclic porphyrin dimer having homotropic allosterism with inhibitory control.
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Chem Commun (Camb),
47,
4246-4248.
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L.M.Hancock,
L.C.Gilday,
N.L.Kilah,
C.J.Serpell,
and
P.D.Beer
(2011).
A new synthetic route to chloride selective [2]catenanes.
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Chem Commun (Camb),
47,
1725-1727.
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M.Elias,
D.Liebschner,
G.Gotthard,
and
E.Chabriere
(2011).
Structural insights and ab initio sequencing within the DING proteins family.
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J Synchrotron Radiat,
18,
45-49.
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F.D.Pitt,
S.Mazard,
L.Humphreys,
and
D.J.Scanlan
(2010).
Functional characterization of Synechocystis sp. strain PCC 6803 pst1 and pst2 gene clusters reveals a novel strategy for phosphate uptake in a freshwater cyanobacterium.
|
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J Bacteriol,
192,
3512-3523.
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L.C.Henderson,
J.Li,
R.L.Nation,
T.Velkov,
and
F.M.Pfeffer
(2010).
Developing an anion host for lipid A binding and antibacterial activity.
|
| |
Chem Commun (Camb),
46,
3197-3199.
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L.M.Hancock,
L.C.Gilday,
S.Carvalho,
P.J.Costa,
V.Félix,
C.J.Serpell,
N.L.Kilah,
and
P.D.Beer
(2010).
Rotaxanes capable of recognising chloride in aqueous media.
|
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Chemistry,
16,
13082-13094.
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P.Ballester
(2010).
Anion binding in covalent and self-assembled molecular capsules.
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Chem Soc Rev,
39,
3810-3830.
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S.O.Kang,
J.M.Llinares,
V.W.Day,
and
K.Bowman-James
(2010).
Cryptand-like anion receptors.
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Chem Soc Rev,
39,
3980-4003.
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W.A.Harrell,
M.L.Bergmeyer,
P.Y.Zavalij,
and
J.T.Davis
(2010).
Ceramide-mediated transport of chloride and bicarbonate across phospholipid membranes.
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Chem Commun (Camb),
46,
3950-3952.
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A.Berna,
F.Bernier,
E.Chabrière,
M.Elias,
K.Scott,
and
A.Suh
(2009).
For whom the bell tolls? DING proteins in health and disease.
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Cell Mol Life Sci,
66,
2205-2218.
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C.Caltagirone,
and
P.A.Gale
(2009).
Anion receptor chemistry: highlights from 2007.
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Chem Soc Rev,
38,
520-563.
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D.Meshcheryakov,
M.Bolte,
and
V.Böhmer
(2009).
Macrocyclic oligoureas with xanthene and diphenyl ether units.
|
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Org Biomol Chem,
7,
4386-4390.
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D.Meshcheryakov,
V.Böhmer,
M.Bolte,
V.Hubscher-Bruder,
and
F.Arnaud-Neu
(2009).
Macrocyclic hexaureas: synthesis, conformation, and anion binding.
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Chemistry,
15,
4811-4821.
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M.J.Chmielewski,
J.J.Davis,
and
P.D.Beer
(2009).
Interlocked host rotaxane and catenane structures for sensing charged guest species via optical and electrochemical methodologies.
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Org Biomol Chem,
7,
415-424.
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R.Pérez-Ruiz,
Y.Díaz,
B.Goldfuss,
D.Hertel,
K.Meerholz,
and
A.G.Griesbeck
(2009).
Fluoride recognition by a chiral urea receptor linked to a phthalimide chromophore.
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Org Biomol Chem,
7,
3499-3504.
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S.Kubik
(2009).
Amino acid containing anion receptors.
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Chem Soc Rev,
38,
585-605.
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A.Berna,
F.Bernier,
E.Chabrière,
T.Perera,
and
K.Scott
(2008).
DING proteins; novel members of a prokaryotic phosphate-binding protein superfamily which extends into the eukaryotic kingdom.
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Int J Biochem Cell Biol,
40,
170-175.
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A.J.Lowe,
and
F.M.Pfeffer
(2008).
Size matters--strong binding of the terephthalate dianion by thiourea functionalised fused [n]polynorbornane hosts.
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Chem Commun (Camb),
(),
1871-1873.
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A.L.Davidson,
E.Dassa,
C.Orelle,
and
J.Chen
(2008).
Structure, function, and evolution of bacterial ATP-binding cassette systems.
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Microbiol Mol Biol Rev,
72,
317.
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C.M.Crane,
A.K.Hirsch,
M.S.Alphey,
T.Sgraja,
S.Lauw,
V.Illarionova,
F.Rohdich,
W.Eisenreich,
W.N.Hunter,
A.Bacher,
and
F.Diederich
(2008).
Synthesis and characterization of cytidine derivatives that inhibit the kinase IspE of the non-mevalonate pathway for isoprenoid biosynthesis.
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ChemMedChem,
3,
91.
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PDB codes:
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J.Ju,
M.Park,
J.M.Suk,
M.S.Lah,
and
K.S.Jeong
(2008).
An anion receptor with NH and OH groups for hydrogen bonds.
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Chem Commun (Camb),
(),
3546-3548.
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M.Vera,
F.Pagliai,
N.Guiliani,
and
C.A.Jerez
(2008).
The chemolithoautotroph Acidithiobacillus ferrooxidans can survive under phosphate-limiting conditions by expressing a C-P lyase operon that allows it to grow on phosphonates.
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Appl Environ Microbiol,
74,
1829-1835.
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A.J.Lowe,
G.A.Dyson,
and
F.M.Pfeffer
(2007).
Steric and electronic factors influencing recognition by a simple, charge neutral norbornene based anion receptor.
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Org Biomol Chem,
5,
1343-1346.
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A.K.Hirsch,
F.R.Fischer,
and
F.Diederich
(2007).
Phosphate recognition in structural biology.
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Angew Chem Int Ed Engl,
46,
338-352.
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M.Tanabe,
O.Mirza,
T.Bertrand,
H.S.Atkins,
R.W.Titball,
S.Iwata,
K.A.Brown,
and
B.Byrne
(2007).
Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains.
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Acta Crystallogr D Biol Crystallogr,
63,
1185-1193.
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PDB codes:
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P.Blondeau,
M.Segura,
R.Pérez-Fernández,
and
J.de Mendoza
(2007).
Molecular recognition of oxoanions based on guanidinium receptors.
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Chem Soc Rev,
36,
198-210.
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S.Moniot,
M.Elias,
D.Kim,
K.Scott,
and
E.Chabriere
(2007).
Crystallization, diffraction data collection and preliminary crystallographic analysis of DING protein from Pseudomonas fluorescens.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
590-592.
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X.X.Zhang,
K.Scott,
R.Meffin,
and
P.B.Rainey
(2007).
Genetic characterization of psp encoding the DING protein in Pseudomonas fluorescens SBW25.
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BMC Microbiol,
7,
114.
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H.Gu,
S.Lalonde,
S.Okumoto,
L.L.Looger,
A.M.Scharff-Poulsen,
A.R.Grossman,
J.Kossmann,
I.Jakobsen,
and
W.B.Frommer
(2006).
A novel analytical method for in vivo phosphate tracking.
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FEBS Lett,
580,
5885-5893.
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K.J.Winstanley,
A.M.Sayer,
and
D.K.Smith
(2006).
Anion binding by catechols--an NMR, optical and electrochemical study.
|
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Org Biomol Chem,
4,
1760-1767.
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M.R.Webb
(2006).
A tale of the unexpected.
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Structure,
14,
391-392.
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R.Morales,
A.Berna,
P.Carpentier,
C.Contreras-Martel,
F.Renault,
M.Nicodeme,
M.L.Chesne-Seck,
F.Bernier,
J.Dupuy,
C.Schaeffer,
H.Diemer,
A.Van-Dorsselaer,
J.C.Fontecilla-Camps,
P.Masson,
D.Rochu,
and
E.Chabriere
(2006).
Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein.
|
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Structure,
14,
601-609.
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PDB code:
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S.O.Kang,
R.A.Begum,
and
K.Bowman-James
(2006).
Amide-based ligands for anion coordination.
|
| |
Angew Chem Int Ed Engl,
45,
7882-7894.
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J.A.Hall,
and
P.C.Maloney
(2005).
Altered oxyanion selectivity in mutants of UhpT, the Pi-linked sugar phosphate carrier of Escherichia coli.
|
| |
J Biol Chem,
280,
3376-3381.
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K.E.Christensen,
I.A.Mirza,
A.M.Berghuis,
and
R.E.Mackenzie
(2005).
Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.
|
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J Biol Chem,
280,
34316-34323.
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PDB code:
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K.J.Chang,
D.Moon,
M.S.Lah,
and
K.S.Jeong
(2005).
Indole-based macrocycles as a class of receptors for anions.
|
| |
Angew Chem Int Ed Engl,
44,
7926-7929.
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M.J.Chmielewski,
and
J.Jurczak
(2005).
Anion recognition by neutral macrocyclic amides.
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Chemistry,
11,
6080-6094.
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S.Kondo,
Y.Hiraoka,
N.Kurumatani,
and
Y.Yano
(2005).
Selective recognition of dihydrogen phosphate by receptors bearing pyridyl moieties as hydrogen bond acceptors.
|
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Chem Commun (Camb),
(),
1720-1722.
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D.B.Sherman,
S.Zhang,
J.B.Pitner,
and
A.Tropsha
(2004).
Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.
|
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Proteins,
56,
828-838.
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M.R.Webb
(2003).
Mycobacterial ABC transport system: structure of the primary phosphate receptor.
|
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Structure,
11,
736-738.
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N.K.Vyas,
M.N.Vyas,
and
F.A.Quiocho
(2003).
Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions.
|
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Structure,
11,
765-774.
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PDB code:
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P.A.Gale
(2003).
A "Holey" supramolecular approach to the detection of enzyme activity.
|
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Chembiochem,
4,
1299-1302.
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T.T.Waldron,
M.A.Modestou,
and
K.P.Murphy
(2003).
Anion binding to a protein-protein complex lacks dependence on net charge.
|
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Protein Sci,
12,
871-874.
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H.C.Huang,
and
J.M.Briggs
(2002).
The association between a negatively charged ligand and the electronegative binding pocket of its receptor.
|
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Biopolymers,
63,
247-260.
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H.Wohlrab,
V.Annese,
and
A.Haefele
(2002).
Single replacement constructs of all hydroxyl, basic, and acidic amino acids identify new function and structure-sensitive regions of the mitochondrial phosphate transport protein.
|
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Biochemistry,
41,
3254-3261.
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R.M.de Lorimier,
J.J.Smith,
M.A.Dwyer,
L.L.Looger,
K.M.Sali,
C.D.Paavola,
S.S.Rizk,
S.Sadigov,
D.W.Conrad,
L.Loew,
and
H.W.Hellinga
(2002).
Construction of a fluorescent biosensor family.
|
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Protein Sci,
11,
2655-2675.
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D.J.Kelly,
and
G.H.Thomas
(2001).
The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea.
|
| |
FEMS Microbiol Rev,
25,
405-424.
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J.S.Marvin,
and
H.W.Hellinga
(2001).
Conversion of a maltose receptor into a zinc biosensor by computational design.
|
| |
Proc Natl Acad Sci U S A,
98,
4955-4960.
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Y.Mao,
J.Chen,
J.A.Maynard,
B.Zhang,
and
F.A.Quiocho
(2001).
A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis.
|
| |
Cell,
104,
433-440.
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PDB code:
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M.R.Gunner,
M.A.Saleh,
E.Cross,
A.ud-Doula,
and
M.Wise
(2000).
Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect.
|
| |
Biophys J,
78,
1126-1144.
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C.Briggs,
L.Mincone,
and
H.Wohlrab
(1999).
Replacements of basic and hydroxyl amino acids identify structurally and functionally sensitive regions of the mitochondrial phosphate transport protein.
|
| |
Biochemistry,
38,
5096-5102.
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R.Novak,
A.Cauwels,
E.Charpentier,
and
E.Tuomanen
(1999).
Identification of a Streptococcus pneumoniae gene locus encoding proteins of an ABC phosphate transporter and a two-component regulatory system.
|
| |
J Bacteriol,
181,
1126-1133.
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D.G.Vassylyev,
H.Tomitori,
K.Kashiwagi,
K.Morikawa,
and
K.Igarashi
(1998).
Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity.
|
| |
J Biol Chem,
273,
17604-17609.
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PDB code:
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D.M.Lawson,
C.E.Williams,
L.A.Mitchenall,
and
R.N.Pau
(1998).
Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.
|
| |
Structure,
6,
1529-1539.
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PDB code:
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M.Brune,
J.L.Hunter,
S.A.Howell,
S.R.Martin,
T.L.Hazlett,
J.E.Corrie,
and
M.R.Webb
(1998).
Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli.
|
| |
Biochemistry,
37,
10370-10380.
|
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P.S.Ledvina,
A.L.Tsai,
Z.Wang,
E.Koehl,
and
F.A.Quiocho
(1998).
Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.
|
| |
Protein Sci,
7,
2550-2559.
|
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PDB code:
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U.Hars,
R.Horlacher,
W.Boos,
W.Welte,
and
K.Diederichs
(1998).
Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose.
|
| |
Protein Sci,
7,
2511-2521.
|
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PDB codes:
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Y.Paas
(1998).
The macro- and microarchitectures of the ligand-binding domain of glutamate receptors.
|
| |
Trends Neurosci,
21,
117-125.
|
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C.M.Bruns,
A.J.Nowalk,
A.S.Arvai,
M.A.McTigue,
K.G.Vaughan,
T.A.Mietzner,
and
D.E.McRee
(1997).
Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily.
|
| |
Nat Struct Biol,
4,
919-924.
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PDB code:
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E.N.Baker
(1997).
Iron-ic twists of fate.
|
| |
Nat Struct Biol,
4,
869-871.
|
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F.A.Quiocho,
J.C.Spurlino,
and
L.E.Rodseth
(1997).
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.
|
| |
Structure,
5,
997.
|
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PDB codes:
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P.Lefèvre,
M.Braibant,
L.de Wit,
M.Kalai,
D.Röeper,
J.Grötzinger,
J.P.Delville,
P.Peirs,
J.Ooms,
K.Huygen,
and
J.Content
(1997).
Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG.
|
| |
J Bacteriol,
179,
2900-2906.
|
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Y.Hu,
S.Rech,
R.P.Gunsalus,
and
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Crystal structure of the molybdate binding protein ModA.
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| |
Nat Struct Biol,
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PDB codes:
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Z.Wang,
H.Luecke,
N.Yao,
and
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(1997).
A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.
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PDB codes:
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A.Phelps,
C.Briggs,
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Biochemistry,
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(1996).
Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.
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| |
Biochemistry,
35,
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PDB codes:
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F.A.Quiocho
(1996).
Atomic basis of the exquisite specificity of phosphate and sulfate transport receptors.
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| |
Kidney Int,
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(1996).
Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.
|
| |
Biochemistry,
35,
2079-2085.
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PDB codes:
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P.S.Ledvina,
N.Yao,
A.Choudhary,
and
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(1996).
Negative electrostatic surface potential of protein sites specific for anionic ligands.
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Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor.
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Crystallization and preliminary X-ray crystallographic analysis of the 38-kDa immunodominant antigen of Mycobacterium tuberculosis.
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The response of the picoplanktonic marine cyanobacterium Synechococcus species WH7803 to phosphate starvation involves a protein homologous to the periplasmic phosphate-binding protein of Escherichia coli.
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Characterization of genes involved in molybdenum transport in Azotobacter vinelandii.
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PDB code:
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Orphan enzyme or patriarch of a new tribe: the arsenic resistance ATPase of bacterial plasmids.
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Gene regulation of plasmid- and chromosome-determined inorganic ion transport in bacteria.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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
codes are
shown on the right.
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