Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases (Q42653986)

4 November 2017

title

Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases (English)

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4 November 2017

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

13 June 2020

author name string

Amit Sharma

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

13 June 2020

publication date

11 April 2014

1 reference

Journal of Structural and Functional Genomics

4 November 2017

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

13 June 2020

volume

15

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

13 June 2020

issue

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

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page(s)

45-61

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

Probing the diverse landscape of protein flexibility and binding

13 June 2020

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A role for both conformational selection and induced fit in ligand binding by the LAO protein

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An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase

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Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses

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Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition

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Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase.

21 January 2018

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Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase.

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Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase

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Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase

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T-Coffee: A novel method for fast and accurate multiple sequence alignment

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The role of dynamic conformational ensembles in biomolecular recognition

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Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state

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Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

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Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases

21 January 2018

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Validation of protein models from Cα coordinates alone

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Enzyme flexibility and enzyme action

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12 December 2020

Conformational selection or induced fit? 50 years of debate resolved

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12 December 2020

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12 December 2020

Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate

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12 December 2020

Correlating amino acid conservation with function in tyrosyl-tRNA synthetase

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Predicting and harnessing protein flexibility in the design of species-specific inhibitors of thymidylate synthase

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12 December 2020

Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles

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12 December 2020

10.1007/S10969-014-9178-X

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24723074 AND SRC:MED&resulttype=core&format=json

13 June 2020

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