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Literature summary for 6.1.1.1 extracted from

  • Datt, M.; Sharma, A.
    Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases (2014), J. Struct. Funct. Genomics, 15, 45-61 .
    View publication on PubMed
Search for more literature for 6.1.1.1

Organism

Organism UniProt Comment Textmining
Leishmania major Q4QFJ7
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Pyrococcus horikoshii O58739
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Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 O58739
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Synonyms

Synonyms Comment Organism
LMJF_14_1370 gene name, UniProt Leishmania major
Tyrosyl-tRNA synthetase
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 Pyrococcus horikoshii
Tyrosyl-tRNA synthetase
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 Leishmania major
YRS
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 Pyrococcus horikoshii
YRS
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 Leishmania major

General Information

General Information Comment Organism
evolution analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview Pyrococcus horikoshii
evolution analysis of evolutionary conservation of KMSKS motif in tyrosyl-tRNA synthetases, YRSs, two YRSs of Pyrococcus horikoshii and Leishmania major have an overall root mean squared deviation calculated as 3.2 A, although the primary sequences for ATP recognition motifs in Pyrococcus horikoshii and Leishmania major YRSs are identical (KMSKS). The KMSKS loop in YRSs is evolutionarily conserved and mediates inter-molecular interactions between YRS and ATP, Conformational landscape of KMSKS loops in YRSs, overview Leishmania major
additional information tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop is very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview Pyrococcus horikoshii
additional information tyrosyl-tRNA synthetase structure comparisons, the KMSKS loop uĆ­s very variable in conformation, intrinsic conformational heterogeneity in KMSKS loop that is independent of occupancy of active site. Differential centroid distance analyses between KMSKS motif and Rossmann fold domain reveal an intriguing bimodal distribution. The KMSKS loop is positioned at the intersection of Rossmann fold and the C-terminal region and plays a role in ATP binding and catalysis. KMSKS loop orientation and conformation can be independent of ATP binding, conformational flexibility of KMSKS loop, overview Leishmania major