High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP.

High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP.

Native data, anomalous data at three wavelengths and an independent peak-wavelength data set for SeMet-substituted protein have been collected from cryoprotected crystals of the TrpRS-adenylate product (TAM) complex to a resolution limit of 1.7 A. Independent phase sets were developed using SHARP an...

Full description

Bibliographic Details
Main Authors:	Retailleau, P, Yin, Y, Hu, M, Roach, J, Bricogne, G, Vonrhein, C, Roversi, P, Blanc, E, Sweet, R, Carter, C
Format:	Journal article
Language:	English
Published:	2001

Similar Items

Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.
by: Retailleau, P, et al.
Published: (2003)

1H and 13C hyperfine coupling constants of the tryptophanyl cation radical in aqueous solution from microsecond time-resolved CIDNP.
by: Kiryutin, A, et al.
Published: (2007)

Ancestral Reconstruction of a Pre-LUCA Aminoacyl-tRNA Synthetase Ancestor Supports the Late Addition of Trp to the Genetic Code
by: Fournier, G. P., et al.
Published: (2016)

Automated structure solution with autoSHARP.
by: Vonrhein, C, et al.
Published: (2007)

Growth-Optimized Aminoacyl-tRNA Synthetase Levels Prevent Maximal tRNA Charging
by: Parker, Darren J., et al.
Published: (2021)

Modelling prior distributions of atoms for macromolecular refinement and completion.
by: Roversi, P, et al.
Published: (2000)

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life
by: Fournier, Gregory P., et al.
Published: (2013)

Amino acid recognition by a Class I tRNA synthetase
by: Schmidt, Eric Thomas
Published: (2005)

Functional analysis of a class II aminoacyl-tRNA synthetase
by: Davis, Matthew W. (Matthew Warren), 1966-
Published: (2005)

Reactions of isoleucyl-tRNA synthetase from Escherichia coli B.
by: Eldred, Emmett Walter.
Published: (2023)

Selective inhibition of divergent seryl-tRNA synthetases by serine analogues.
by: Ahel, D, et al.
Published: (2005)

Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT.
by: Blanc, E, et al.
Published: (2004)

Prolyl-tRNA synthetase as a novel therapeutic target in multiple myeloma
by: Kurata, K, et al.
Published: (2023)

Characterizing the landscape of aminoacyl-tRNA synthetase protein production in Bacillus subtilis
by: Parker, Darren John.
Published: (2021)

Analogs of natural aminoacyl-tRNA synthetase inhibitors clear malaria in vivo
by: Camacho, Noelia, et al.
Published: (2015)

Incorporation of Fluorotyrosines into Ribonucleotide Reductase Using an Evolved, Polyspecific Aminoacyl-tRNA Synthetase
by: Young, Douglas D., et al.
Published: (2013)

Drug targeting of one or more aminoacyl-tRNA synthetase in the malaria parasite Plasmodium falciparum
by: Manickam, Y, et al.
Published: (2018)

In-house low-resolution X-ray crystallography.
by: Evans, G, et al.
Published: (2000)

Dimerization of arginyl-tRNA synthetase by free heme drives its inactivation in plasmodium falciparum
by: Jain, V, et al.
Published: (2016)

Compound heterozygosity for loss-of-function lysyl-tRNA synthetase mutations in a patient with peripheral neuropathy.
by: McLaughlin, H, et al.
Published: (2010)

Reaction hijacking of tyrosine tRNA synthetase as a new whole-of-life-cycle antimalarial strategy
by: Niles, Jacquin
Published: (2023)

A Loss-of-Function Variant in the Human Histidyl-tRNA Synthetase (HARS) Gene is Neurotoxic In Vivo
by: Vester, A, et al.
Published: (2013)

A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo.
by: Vester, A, et al.
Published: (2013)

Targeting prolyl-tRNA synthetase to accelerate drug discovery against malaria, leishmaniasis, toxoplasmosis, cryptosporidiosis, and coccidiosis.
by: Jain, V, et al.
Published: (2017)

The cytoplasmic prolyl-tRNA synthetase of the malaria parasite is a dual-stage target of febrifugine and its analogs
by: Pepper, L. R., et al.
Published: (2016)

Life without tRNA[superscript Ile]-lysidine synthetase: translation of the isoleucine codon AUA in Bacillus subtilis lacking the canonical tRNA[Ile over 2]
by: Koehrer, Caroline, et al.
Published: (2013)

Impaired protein translation in Drosophila models for Charcot–Marie–Tooth neuropathy caused by mutant tRNA synthetases
by: Niehues, Sven, et al.
Published: (2015)

Structure of prolyl-tRNA synthetase-halofuginone complex provides basis for development of drugs against malaria and toxoplasmosis
by: Jain, V, et al.
Published: (2015)

Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition.
by: Bilokapic, S, et al.
Published: (2006)

Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy.
by: Cader, M, et al.
Published: (2007)

Repositioning and Characterization of 1-(Pyridin-4-yl)pyrrolidin-2-one Derivatives as Plasmodium Cytoplasmic Prolyl-tRNA Synthetase Inhibitors
by: Okaniwa, Masanori, et al.
Published: (2021)

Igf2 pathway dependency of the Trp53 developmental and tumour phenotypes.
by: Haley, V, et al.
Published: (2012)

The mechanism of ACV synthetase
by: Byford, M, et al.
Published: (1997)

The Mechanism of ACV Synthetase.
by: Byford, M, et al.
Published: (1997)

Designed Trp/Arg-rich antimicrobial peptides.
by: Giam, Zhen Gan.
Published: (2013)

TIR domains of plant immune receptors are 2',3'-cAMP/cGMP synthetases mediating cell death
by: Yu, Dongli, et al.
Published: (2023)

A Recurrent Loss-of-Function Alanyl-tRNA Synthetase (AARS) Mutation in Patients with Charcot-Marie-Tooth Disease Type 2N (CMT2N)
by: McLaughlin, H, et al.
Published: (2012)

A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
by: McLaughlin, H, et al.
Published: (2012)

A Recurrent Loss-of-Function Alanyl-tRNA Synthetase (AARS) Mutation in Patients with Charcot-Marie-Tooth Disease Type 2N (CMT2N)
by: Mclaughlin, H, et al.
Published: (2014)

A Recurrent Loss-of-Function Alanyl-tRNA Synthetase (AARS) Mutation in Patients with Charcot-Marie-Tooth Disease Type 2N (CMT2N)
by: Mclaughlin, H, et al.
Published: (2014)