Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation - Wikidata - awgldk - TriplyDB

Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation

Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation

http://www.wikidata.org/entity/Q34352343

about

Urzymology: experimental access to a key transition in the appearance of enzymes What RNA World? Why a Peptide/RNA Partnership Merits Renewed Experimental Attention Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens Anticodon Modifications in the tRNA Set of LUCA and the Fundamental Regularity in the Standard Genetic Code The place of RNA in the origin and early evolution of the genetic machinery Structural phylogenomics retrodicts the origin of the genetic code and uncovers the evolutionary impact of protein flexibility The Rodin-Ohno hypothesis that two enzyme superfamilies descended from one ancestral gene: an unlikely scenario for the origins of translation that will not be dismissed.An Ancestral Tryptophanyl-tRNA Synthetase Precursor Achieves High Catalytic Rate Enhancement without Ordered Ground-State Tertiary Structures.High-Dimensional Mutant and Modular Thermodynamic Cycles, Molecular Switching, and Free Energy Transduction.Coordination of tRNA synthetase active sites for chemical fidelity Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation.tRNA acceptor stem and anticodon bases form independent codes related to protein folding.Statistical evaluation of the Rodin-Ohno hypothesis: sense/antisense coding of ancestral class I and II aminoacyl-tRNA synthetases.Aminoacylating urzymes challenge the RNA world hypothesis Full implementation of the genetic code by tryptophanyl-tRNA synthetase requires intermodular coupling Enhanced amino acid selection in fully evolved tryptophanyl-tRNA synthetase, relative to its urzyme, requires domain motion sensed by the D1 switch, a remote dynamic packing motif.Combining multi-mutant and modular thermodynamic cycles to measure energetic coupling networks in enzyme catalysis.Enzyme recruitment and its role in metabolic expansion.A master switch couples Mg²⁺-assisted catalysis to domain motion in B. stearothermophilus tryptophanyl-tRNA Synthetase Evolutionary importance of the intramolecular pathways of hydrolysis of phosphate ester mixed anhydrides with amino acids and peptides.Interdependence, Reflexivity, Fidelity, Impedance Matching, and the Evolution of Genetic Coding.Coding of Class I and II Aminoacyl-tRNA Synthetases.The evolution of Class II Aminoacyl-tRNA synthetases and the first code.A Proposal of the Ur-proteome.

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P2860

Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation

http://www.wikidata.org/entity/Q34352343

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@ast

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@en

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@nl

type

label

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@ast

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

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Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@nl

prefLabel

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@ast

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@en

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

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P356

JBC.M110.136911

P1433

Journal of Biological Chemistry

P1476

Tryptophanyl-tRNA synthetase U ...... intramolecular complementation

@en

P2093

Brian Kuhlman

http://www.w3.org/2001/XMLSchema#string

Charles W Carter

http://www.w3.org/2001/XMLSchema#string

Glenn L Butterfoss

http://www.w3.org/2001/XMLSchema#string

Hao Hu

http://www.w3.org/2001/XMLSchema#string

Violetta Weinreb

http://www.w3.org/2001/XMLSchema#string

Yen Pham

http://www.w3.org/2001/XMLSchema#string

P2860

The Pfam protein families database

Crystal structure of an ancient protein: evolution by conformational epistasis

RosettaDesign server for protein design

Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations

Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants

Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase

A rationally engineered misacylating aminoacyl-tRNA synthetase

An epistatic ratchet constrains the direction of glucocorticoid receptor evolution

The CCP4 suite: programs for protein crystallography

An expanded eukaryotic genetic code

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38590-38601

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scholarly article

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10.1074/JBC.M110.136911

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49

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285

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2010-09-23T00:00:00Z

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46413843

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20864539

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2992291

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