Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions (Q34100973)

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English	Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions	scientific article

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scholarly article

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Europe PubMed Central

31 July 2017

Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions (English)

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Europe PubMed Central

31 July 2017

object named as

Pierre Barraud

2

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Carine Tisné

3

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author name string

Amandine Guelorget

1

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Europe PubMed Central

31 July 2017

Béatrice Golinelli-Pimpaneau

4

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Europe PubMed Central

31 July 2017

publication date

14 December 2011

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Europe PubMed Central

31 July 2017

BMC Structural Biology

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Europe PubMed Central

31 July 2017

11

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Europe PubMed Central

31 July 2017

48

1 reference

Europe PubMed Central

31 July 2017

https://scigraph.springernature.com/pub.10.1186/1472-6807-11-48

0 references

Thermophilic proteins: insight and perspective from in silico experiments

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Mechanism-based strategies for trapping and crystallizing complexes of RNA-modifying enzymes

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Thermostability in endoglucanases is fold-specific

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Discrimination of thermophilic and mesophilic proteins

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Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase

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Crystal structure of a thermostable old yellow enzyme from Thermus scotoductus SA-01

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The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation

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Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNA

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Implication for buried polar contacts and ion pairs in hyperthermostable enzymes

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Lessons in stability from thermophilic proteins

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The genomics of disulfide bonding and protein stabilization in thermophiles

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The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans

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Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability

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Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase

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A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase

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Many paths to methyltransfer: a chronicle of convergence

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Cloning and characterization of tRNA (m1A58) methyltransferase (TrmI) from Thermus thermophilus HB27, a protein required for cell growth at extreme temperatures

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Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile

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Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases

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In silico analysis of the tRNA:m1A58 methyltransferase family: homology-based fold prediction and identification of new members from Eubacteria and Archaea

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How do thermophilic proteins deal with heat?

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Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv

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Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase

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Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability

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The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds

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Oligomeric integrity--the structural key to thermal stability in bacterial alcohol dehydrogenases

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Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability

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The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges.

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The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.

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Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase

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The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins

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Elucidation of determinants of protein stability through genome sequence analysis.

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Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding

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Structural and Genomic Correlates of Hyperthermostability

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Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat"

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10.1186/1472-6807-11-48

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Europe PubMed Central

31 July 2017

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mapped directly with Wikidata item

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Europe PubMed Central

31 July 2017

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Europe PubMed Central

31 July 2017

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