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PDBsum entry 2j5b
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References listed in PDB file
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Key reference
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Title
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Virus-Encoded aminoacyl-Trna synthetases: structural and functional characterization of mimivirus tyrrs and metrs.
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Authors
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C.Abergel,
J.Rudinger-Thirion,
R.Giegé,
J.M.Claverie.
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Ref.
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J Virol, 2007,
81,
12406-12417.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is
translated in amino acids and in providing the substrate for protein synthesis.
As such, they fulfill a key role in a process universally conserved in all
cellular organisms from their most complex to their most reduced parasitic
forms. In contrast, even complex viruses were not found to encode much
translation machinery, with the exception of isolated components such as tRNAs.
In this context, the discovery of four aminoacyl-tRNA synthetases encoded in the
genome of mimivirus together with a full set of translation initiation,
elongation, and termination factors appeared to blur what was once a clear
frontier between the cellular and viral world. Functional studies of two
mimivirus tRNA synthetases confirmed the MetRS specificity for methionine and
the TyrRS specificity for tyrosine and conformity with the identity rules for
tRNA(Tyr) for archea/eukarya. The atomic structure of the mimivirus tyrosyl-tRNA
synthetase in complex with tyrosinol exhibits the typical fold and active-site
organization of archaeal-type TyrRS. However, the viral enzyme presents a unique
dimeric conformation and significant differences in its anticodon binding site.
The present work suggests that mimivirus aminoacyl-tRNA synthetases function as
regular translation enzymes in infected amoebas. Their phylogenetic
classification does not suggest that they have been acquired recently by
horizontal gene transfer from a cellular host but rather militates in favor of
an intricate evolutionary relationship between large DNA viruses and ancestral
eukaryotes.
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Secondary reference #1
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Title
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Mimivirus tyrrs: preliminary structural and functional characterization of the first amino-Acyl tRNA synthetase found in a virus.
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Authors
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C.Abergel,
S.Chenivesse,
D.Byrne,
K.Suhre,
V.Arondel,
J.M.Claverie.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005,
61,
212-215.
[DOI no: ]
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PubMed id
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Figure 1.
Enzymatic activity of mimivirus TyrRS versus E. coli TyrRS.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 February
1; 61(Pt 2): 212–215. Published online 2005 January 20. doi:
10.1107/S174430910500062X. Copyright [copyright] International
Union of Crystallography 2005
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Figure 2.
Multiple alignment of the mimivirus TyrRS sequence with
structural homologues and related archeal and eukaryotic
sequences. j1u and n3l correspond to the PDB structures
http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1j1u (Kobayashi et
al., 2003[triangle]) and
http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1n3l (Yang et al.,
2002[triangle]). The accession numbers of the homologous
sequences are as follow: Ehisto, Entamoeba histolytica
unfinished genome (gnl|TIGR_5759, ENTER63TR); Osati, Oryza
sativa putative TyrRS (Q84PX0); Atha1, Arabidopsis thaliana
putative TyrsRS (Q8S9J2); Atha2, Arabidopsis thaliana putative
TyrsRS (P93018); Tobac, Nicotiana tabacum putative TyrRS
(P93363); Pyoeli, Plasmodium yoelii putative TyrRS (Q7RH02);
CParvum, Cryptosporidium parvum putative TyrRS(Q7YYA0). Black
triangles correspond to residues known to be involved in
interaction with the tyrosine, green triangles correspond to
residues known to be involved in interaction with the acceptor
and red stars correspond to residues known to be involved in
interaction with the anticodon. The multiple alignment was
generated using the T-COFFEE software (Poirot et al.,
2004[triangle]) in order to combine structural and sequence
information and was used through the CaspR procedure to generate
homology-based models of the mimivirus structure. Acta
Crystallogr Sect F Struct Biol Cryst Commun. 2005 February 1;
61(Pt 2): 212–215. Published online 2005 January 20. doi:
10.1107/S174430910500062X. Copyright [copyright] International
Union of Crystallography 2005
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by the IUCr
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