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Literature DB >> 21784948

A molecular basis for tungstate selectivity in prokaryotic ABC transport systems.

Loes E Bevers¹, Guenter Schwarz, Wilfred R Hagen.

Abstract

The essential trace compounds tungstate and molybdate are taken up by cells via ABC transporters. Despite their similar ionic radii and chemical properties, the WtpA protein selectively binds tungstate in the presence of molybdate. Using site-directed mutagenesis of conserved binding pocket residues, we established a molecular basis for tungstate selectivity.

Entities: Chemical

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Year: 2011 PMID： 21784948 PMCID： PMC3165707 DOI： 10.1128/JB.05056-11

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

11 in total

1. Oxyanion selectivity in sulfate and molybdate transport proteins: an ab initio/CDM study.

Authors: Todor Dudev; Carmay Lim
Journal: J Am Chem Soc Date: 2004-08-25 Impact factor: 15.419

2. The molybdate binding protein Mop from Haemophilus influenzae--biochemical and thermodynamic characterisation.

Authors: Seth L Masters; Geoffrey J Howlett; Richard N Pau
Journal: Arch Biochem Biophys Date: 2005-07-01 Impact factor: 4.013

3. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters.

Authors: Loes E Bevers; Peter-Leon Hagedoorn; Gerard C Krijger; Wilfred R Hagen
Journal: J Bacteriol Date: 2006-09 Impact factor: 3.490

4. Structure of an ABC transporter in complex with its binding protein.

Authors: Kaspar Hollenstein; Dominik C Frei; Kaspar P Locher
Journal: Nature Date: 2007-02-25 Impact factor: 49.962

Review 5. Tungsten, the surprisingly positively acting heavy metal element for prokaryotes.

Authors: Jan R Andreesen; Kathrin Makdessi
Journal: Ann N Y Acad Sci Date: 2007-12-20 Impact factor: 5.691

6. Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.

Authors: D M Lawson; C E Williams; L A Mitchenall; R N Pau
Journal: Structure Date: 1998-12-15 Impact factor: 5.006

A molecular basis for tungstate selectivity in prokaryotic ABC transport systems.

1. Oxyanion selectivity in sulfate and molybdate transport proteins: an ab initio/CDM study.

2. The molybdate binding protein Mop from Haemophilus influenzae--biochemical and thermodynamic characterisation.

3. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters.

4. Structure of an ABC transporter in complex with its binding protein.

Review 5. Tungsten, the surprisingly positively acting heavy metal element for prokaryotes.

6. Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.

7. Tungstate Uptake by a highly specific ABC transporter in Eubacterium acidaminophilum.

8. Molybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system.

9. Distorted octahedral coordination of tungstate in a subfamily of specific binding proteins.

10. Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli.

1. TupA: a tungstate binding protein in the periplasm of Desulfovibrio alaskensis G20.

2. Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20.