Journal ArticleDOI
A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
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TLDR
The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described, and is the first representative of a second class of aminoacyl-tRNA synthet enzyme structures.Abstract:
The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 A resolution, is described. It has an N-terminal domain that forms an antiparallel α helical coiled-coil, stretching 60 A out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site α – β domain based around a seven-stranded antiparallel β sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding fold, and is the first representative of a second class of aminoacyl-tRNA synthetase structures.read more
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Predicting coiled coils from protein sequences
TL;DR: This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.
Journal ArticleDOI
Molecular Physiology of P2X Receptors
TL;DR: P2X receptors are membrane ion channels that open in response to the binding of extracellular ATP and are involved in the initiation of afferent signals in several viscera and play a key role in sensing tissue-damaging and inflammatory stimuli.
Journal ArticleDOI
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.
TL;DR: The crystal structure of the GCN4Leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
Journal ArticleDOI
Coiled coils - new structures and new functions
TL;DR: The structures of more than 20 proteins containing coiled-coil domains have been solved to high resolution and provided many new insights into the structure of coiled coils, their discontinuities, their relationship with other helical bundles and the problems connected with their prediction from protein sequences.
Journal ArticleDOI
Aminoacyl-tRNA synthesis.
Michael Ibba,Dieter Söll +1 more
TL;DR: Current knowledge of the biochemical, structural, and evolutionary facets of aminoacyl-tRNA synthesis is reviewed, mainly prompted by the advent of whole genome sequencing and the availability of vast body of structural data.
References
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Journal ArticleDOI
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
Wolfgang Kabsch,Chris Sander +1 more
TL;DR: A set of simple and physically motivated criteria for secondary structure, programmed as a pattern‐recognition process of hydrogen‐bonded and geometrical features extracted from x‐ray coordinates is developed.
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The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Chemical and biological evolution of nucleotide-binding protein.
TL;DR: Three-dimensional alignment of the common nucleotide binding structure in dehydrogenases, kinases and flavodoxins permits the recognition of homologous amino acids when sequence comparisons alone would fail.
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Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
TL;DR: Surprisingly, this partition of aaRS in two classes is found to be strongly correlated on the functional level with the acylation occurring either on the 2′ OH or 3′ OH of the ribose of the last nucleotide of tRNA.
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Scissors-grip model for DNA recognition by a family of leucine zipper proteins
TL;DR: An evaluation of the properties of conserved amino acids within the basic region of 11 deduced protein sequences, coupled with the observation that they are located at an invariant distance from the leucine zipper, has led to the formulation of a "scissors-grip" model for DNA binding.