Emily R. Featherston
Pennsylvania State University
Heterologous expressionHydrogen bondSelectivityMutagenesisEnzymeChemistryCofactorPeriplasmic spaceLanthanideCombinatorial chemistryElectron transport chainMethylobacterium extorquensMethylotrophConformational changeCarboxylatePyrroloquinoline quinoneMethanol dehydrogenaseAlanineCytochromeCharacterization (materials science)Cytochrome cEF handATP-binding cassette transporterPlasma protein bindingMetalEscherichia coliBinding proteinBiochemistryRedoxComputational biologyStereochemistryProtein purification
6Publications
4H-index
100Citations
Publications 8
Newest
#1Stephanie Liu (University of Texas at Austin)H-Index: 1
#2Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
The biological importance of lanthanides, and the early lanthanides (La3+–Nd3+) in particular, has only recently been recognized, and the structural principles underlying selective binding of lanthanide ions in biology are not yet well established. Lanmodulin (LanM) is a novel protein that displays unprecedented affinity and selectivity for lanthanides over most other metal ions, with an uncommon preference for the early lanthanides. Its utilization of EF-hand motifs to bind lanthanides, rather ...
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#1Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
#2Edward J. Issertell (PSU: Pennsylvania State University)H-Index: 1
Last. Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
view all 3 authors...
Lanmodulin is the first natural, selective macrochelator for f elements-a protein that binds lanthanides with picomolar affinity at 3 EF hands, motifs that instead bind calcium in most other proteins. Here, we use sensitized terbium luminescence to probe the mechanism of lanthanide recognition by this protein as well as to develop a terbium-specific biosensor that can be applied directly in environmental samples. By incorporating tryptophan residues into specific EF hands, we infer the order of ...
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#1Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
#2Joseph A. Mattocks (PSU: Pennsylvania State University)H-Index: 4
Last. Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
view all 4 authors...
Recent work has revealed that certain lanthanides-in particular, the more earth-abundant, lighter lanthanides-play essential roles in pyrroloquinoline quinone (PQQ) dependent alcohol dehydrogenases from methylotrophic and non-methylotrophic bacteria. More recently, efforts of several laboratories have begun to identify the molecular players (the lanthanome) involved in selective uptake, recognition, and utilization of lanthanides within the cell. In this chapter, we present protocols for the het...
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#1Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
#2Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
Lanthanides are relative newcomers to the field of cell biology of metals; their specific incorporation into enzymes was only demonstrated in 2011, with the isolation of a bacterial lanthanide- and pyrroloquinoline quinone-dependent methanol dehydrogenase. Since that discovery, the efforts of many investigators have revealed that lanthanide utilization is widespread in environmentally important bacteria, and parallel efforts have focused on elucidating the molecular details involved in selective...
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#1Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
#2Hannah R. Rose (PSU: Pennsylvania State University)H-Index: 5
Last. Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
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: Lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have recently been shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems contain two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function), about which little is known. In this work, we have biochemically and structurally characterized these proteins from the methyltroph Methylobacterium extorquens AM1. In contrast to results obtained in a...
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#2Hannah R. RoseH-Index: 5
Last. Joseph A. CotruvoH-Index: 18
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#1Erik C. Cook (PSU: Pennsylvania State University)H-Index: 9
#2Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
Last. Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
view all 4 authors...
Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with CaII binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for LnIIIs and YIII over CaII. Here we present the nuclear magnetic resonance solution structure of LanM complexed wit...
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#1Joseph A. Cotruvo (PSU: Pennsylvania State University)H-Index: 18
#2Emily R. Featherston (PSU: Pennsylvania State University)H-Index: 4
Last. Tatiana N. Laremore (PSU: Pennsylvania State University)H-Index: 23
view all 5 authors...
Lanthanides (Lns) have been shown recently to be essential cofactors in certain enzymes in methylotrophic bacteria. Here we identify in the model methylotroph, Methylobacterium extorquens, a highly selective LnIII-binding protein, which we name lanmodulin (LanM). LanM possesses four metal-binding EF hand motifs, commonly associated with CaII-binding proteins. In contrast to other EF hand-containing proteins, however, LanM undergoes a large conformational change from a largely disordered state to...
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