A comprehensive binding study illustrates ligand recognition in the periplasmic binding protein PotF

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli.

Journal of Bacteriology ◽

10.1128/jb.171.5.2626-2633.1989 ◽

1989 ◽

Vol 171 (5) ◽

pp. 2626-2633 ◽

Cited By ~ 102

Author(s):

H Staudenmaier ◽

B Van Hove ◽

Z Yaraghi ◽

V Braun

Keyword(s):

Escherichia Coli ◽

Transport Mechanism ◽

Binding Protein ◽

Nucleotide Sequences ◽

Periplasmic Binding Protein ◽

Dependent Transport

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Study on the mechanism of the BtuF periplasmic-binding protein for vitamin B12

Biophysical Chemistry ◽

10.1016/j.bpc.2008.02.017 ◽

2008 ◽

Vol 135 (1-3) ◽

pp. 19-24 ◽

Cited By ~ 14

Author(s):

Ming Liu ◽

TingGuang Sun ◽

JianPing Hu ◽

WeiZu Chen ◽

CunXin Wang

Keyword(s):

Vitamin B12 ◽

Binding Protein ◽

Periplasmic Binding Protein

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Trapping open and closed forms of FitE-A group III periplasmic binding protein

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.22272 ◽

2009 ◽

Vol 75 (3) ◽

pp. 598-609 ◽

Cited By ~ 24

Author(s):

Rong Shi ◽

Ariane Proteau ◽

John Wagner ◽

Qizhi Cui ◽

Enrico O. Purisima ◽

...

Keyword(s):

Binding Protein ◽

Periplasmic Binding Protein ◽

Group Iii

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Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli.

Journal of Bacteriology ◽

10.1128/jb.175.20.6546-6552.1993 ◽

1993 ◽

Vol 175 (20) ◽

pp. 6546-6552 ◽

Cited By ~ 41

Author(s):

D Hekstra ◽

J Tommassen

Keyword(s):

Escherichia Coli ◽

Binding Protein ◽

Transport Systems ◽

Periplasmic Binding Protein ◽

Abc Proteins ◽

Dependent Transport

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Characterization of a Sinorhizobium melilotiATP-Binding Cassette Histidine Transporter Also Involved in Betaine and Proline Uptake

Journal of Bacteriology ◽

10.1128/jb.182.13.3717-3725.2000 ◽

2000 ◽

Vol 182 (13) ◽

pp. 3717-3725 ◽

Cited By ~ 31

Author(s):

Eric Boncompagni ◽

Laurence Dupont ◽

Tam Mignot ◽

Magne Østeräs ◽

Annie Lambert ◽

...

Keyword(s):

Glycine Betaine ◽

Sinorhizobium Meliloti ◽

Binding Protein ◽

Compatible Solutes ◽

Site Directed Mutagenesis ◽

Uptake System ◽

Periplasmic Binding Protein ◽

Gene Encoding ◽

Inhibition Of Growth

ABSTRACT The symbiotic soil bacterium Sinorhizobium melilotiuses the compatible solutes glycine betaine and proline betaine for both protection against osmotic stress and, at low osmolarities, as an energy source. A PCR strategy based on conserved domains in components of the glycine betaine uptake systems from Escherichia coli(ProU) and Bacillus subtilis (OpuA and OpuC) allowed us to identify a highly homologous ATP-binding cassette (ABC) binding protein-dependent transporter in S. meliloti. This system was encoded by three genes (hutXWV) of an operon which also contained a fourth gene (hutH2) encoding a putative histidase, which is an enzyme involved in the first step of histidine catabolism. Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake. These mutants showed a 50% reduction in high-affinity uptake of histidine, proline, and proline betaine and about a 30% reduction in low-affinity glycine betaine transport. When histidine was used as a nitrogen source, a 30% inhibition of growth was observed inhut mutants (hutX and hutH2). Expression analysis of the hut operon determined using ahutX-lacZ fusion revealed induction by histidine, but not by salt stress, suggesting this uptake system has a catabolic role rather than being involved in osmoprotection. To our knowledge, Hut is the first characterized histidine ABC transporter also involved in proline and betaine uptake.

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