A Genetically Encoded Bidentate, Metal‐Binding Amino Acid

Xie, Jianming; Liu, Wenshe Ray; Schultz, Peter G.

doi:10.1002/anie.200703397

Cited by 144 publications

(119 citation statements)

References 31 publications

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“…The crystal structure of BpyRS complexed with Bpy-Ala showed that the amino acid binding site could accommodate the extra two carbons of Phen-Ala (Figure 2). 10 The structure also showed that the two pyridine rings in Bpy-Ala are not on the same plan; one of the rings was twisted at 21 degree, while the Phen ring has a planar structure. However, we expected that BpyRS might still recognize and aminoacylate Phen-Ala to the corresponding tRNA.…”

Section: Resultsmentioning

confidence: 98%

Genetic Incorporation of a Phenanthroline-Containing Amino Acid in Escherichia coli

Jin¹,

Lee²,

Lee³

et al. 2014

Bulletin of the Korean Chemical Society

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A simple and general method that selectively introduces metal binding sites into a protein can greatly increase the ability to design and biosynthesize artificial metalloproteins. Here, we report the incorporation of a phenanthroline-containing amino acid (Phen-Ala) into proteins in Escherichia coli by using the tRNA Tyr CUAand tyrosyl aminoacyl-tRNA synthetase pair (BpyRS) from Methanococcus jannaschii, which was originally developed for a bipyridine-containing amino acid (Bpy-Ala). The incorporation efficiency of BpyRS for PhenAla was comparable to that for Bpy-Ala. Because of its high metal-binding ability and characteristic spectral properties, Phen-Ala can be a useful alternative to the existing metal-chelating amino acids for the design and synthesis of artificial metalloproteins.

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Section: Resultsmentioning

confidence: 98%

Genetic Incorporation of a Phenanthroline-Containing Amino Acid in Escherichia coli

Jin¹,

Lee²,

Lee³

et al. 2014

Bulletin of the Korean Chemical Society

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“…2 (37)) and (2,2′-bipyridin-5-yl)alanine ( Fig. 2 (38)), can be readily incorporated into proteins in E. coli [121,122]. Heavy metal cations can be loaded, and their scattering may also be used to solve the phase.…”

Section: Applications In X-ray Crystallographymentioning

confidence: 99%

Biochemical analysis with the expanded genetic lexicon

2012

Anal Bioanal Chem

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The information used to build proteins is stored in the genetic material of every organism. In nature, ribosomes use 20 native amino acids to synthesize proteins in most circumstances. However, laboratory efforts to expand the genetic repertoire of living cells and organisms have successfully encoded more than 80 nonnative amino acids in E. coli, yeast, and other eukaryotic systems. The selectivity, fidelity, and site-specificity provided by the technology have enabled unprecedented flexibility in manipulating protein sequences and functions in cells. Various biophysical probes can be chemically conjugated or directly incorporated at specific residues in proteins, and corresponding analytical techniques can then be used to answer diverse biological questions. This review summarizes the methodology of genetic code expansion and its recent progress, and discusses the applications of commonly used analytical methods.

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“…This has allowed structure and multimer formation of Cu(I)-binding proteins to be explored, as the nitroxide interactions are not influenced by the presence of diamagnetic Cu(I) [31]. Introduction of paramagnetic copper sites into proteins has utilized genetically encoded artificial ligands [36], sitedirected mutation to introduce histidine residues [33] or the incorporation of sequences known to coordinate Cu(II) [34,35]. The addition of sequences based on copper sites from the prion protein (viz.…”

Section: Paramagnetic Copper and Nitroxide Spin-labelsmentioning

confidence: 99%

Nitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function

Jones

Berliner

2016

Cell Biochem Biophys

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Copper is one of the most abundant biological metals, and its chemical properties mean that organisms need sophisticated and multilayer mechanisms in place to maintain homoeostasis and avoid deleterious effects. Studying copper proteins requires multiple techniques, but electron paramagnetic resonance (EPR) plays a key role in understanding Cu(II) sites in proteins. When spin-labels such as aminoxyl radicals (commonly referred to as nitroxides) are introduced, then EPR becomes a powerful technique to monitor not only the coordination environment, but also to obtain structural information that is often not readily available from other techniques. This information can contribute to explaining how cuproproteins fold and misfold. The theory and practice of EPR can be daunting to the non-expert; therefore, in this mini review, we explore how nitroxide spin-labelling can be used to help the inorganic biochemist gain greater understanding of cuproprotein structure and function in vitro and how EPR imaging may help improve understanding of copper homoeostasis in vivo.

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A Genetically Encoded Bidentate, Metal‐Binding Amino Acid

Cited by 144 publications

References 31 publications

Genetic Incorporation of a Phenanthroline-Containing Amino Acid in Escherichia coli

Genetic Incorporation of a Phenanthroline-Containing Amino Acid in Escherichia coli

Biochemical analysis with the expanded genetic lexicon

Nitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function

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