Carmen Berthet-Colominas

TL;DR: 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.

TL;DR: The crystal structure of the EF- Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å and the interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF -Tu for guanine nucleotides.

TL;DR: A novel head‐to‐tail dimer of p24 molecules which occurs through the formation of a substantial intermolecular interface between the N‐ and C‐terminal domains is observed, revealing a remarkable stickiness and plasticity of the p24 molecule.

TL;DR: Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of Seryl adenylate have been determined at 2.5 A resolution, finding four regions in the primary sequence involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases.

TL;DR: The comparison of the two structures indicates increased hydrophobicity, reduced conformational entropy and reduced torsional strain as possible mechanisms by which thermostability is obtained in the enzyme from the thermophile.