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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58739

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Pyrococcus horikoshii
UNIPROT: O58739 not found.
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, cyt-18 protein, tyrosyl trna synthetase, mttyrrs, ldtyrrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tyrosyl-tRNA synthetase
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Tyrosine translase
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Tyrosine tRNA synthetase
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Tyrosine--tRNA ligase
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Tyrosine-transfer ribonucleate synthetase
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Tyrosine-transfer RNA ligase
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Tyrosyl--tRNA ligase
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Tyrosyl-transfer ribonucleate synthetase
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Tyrosyl-transfer ribonucleic acid synthetase
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Tyrosyl-transfer RNA synthetase
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Tyrosyl-tRNA ligase
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Tyrosyl-tRNA synthetase
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TyrRS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Acylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 74.35 A, b = 88.26 A, c = 162.92 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuratani, M.; Sakai, H.; Takahashi, M.; Yanagisawa, T.; Kobayashi, T.; Murayama, K.; Chen, L.; Liu, Z.J.; Wang, B.C.; Kuroishi, C.; Kuramitsu, S.; Terada, T.; Bessho, Y.; Shirouzu, M.; Sekine, S.; Yokoyama, S.
Crystal structures of tyrosyl-tRNA synthetases from Archaea
J. Mol. Biol.
355
395-408
2006
Archaeoglobus fulgidus (O29482), Archaeoglobus fulgidus, Pyrococcus horikoshii (O58739), Pyrococcus horikoshii, Aeropyrum pernix (Q9YA64), Aeropyrum pernix
Manually annotated by BRENDA team
Datt, M.; Sharma, A.
Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases
J. Struct. Funct. Genomics
15
45-61
2014
Pyrococcus horikoshii (O58739), Leishmania major (Q4QFJ7), Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 (O58739)
Manually annotated by BRENDA team