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PDBsum entry 1htt
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Complex (tRNA synthetase/his-adenylate)
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PDB id
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1htt
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of histidyl-Trna synthetase from escherichia coli complexed with histidyl-Adenylate.
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Authors
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J.G.Arnez,
D.C.Harris,
A.Mitschler,
B.Rees,
C.S.Francklyn,
D.Moras.
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Ref.
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Embo J, 1995,
14,
4143-4155.
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PubMed id
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Abstract
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The crystal structure at 2.6 A of the histidyl-tRNA synthetase from Escherichia
coli complexed with histidyl-adenylate has been determined. The enzyme is a
homodimer with a molecular weight of 94 kDa and belongs to the class II of
aminoacyl-tRNA synthetases (aaRS). The asymmetric unit is composed of two
homodimers. Each monomer consists of two domains. The N-terminal catalytic core
domain contains a six-stranded antiparallel beta-sheet sitting on two
alpha-helices, which can be superposed with the catalytic domains of yeast
AspRS, and GlyRS and SerRS from Thermus thermophilus with a root-mean-square
difference on the C alpha atoms of 1.7-1.9 A. The active sites of all four
monomers are occupied by histidyl-adenylate, which apparently forms during
crystallization. The 100 residue C-terminal alpha/beta domain resembles half of
a beta-barrel, and provides an independent domain oriented to contact the
anticodon stem and part of the anticodon loop of tRNA(His). The modular domain
organization of histidyl-tRNA synthetase reiterates a repeated theme in aaRS,
and its structure should provide insight into the ability of certain aaRS to
aminoacylate minihelices and other non-tRNA molecules.
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Secondary reference #1
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Title
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Crystallization of histidyl-Trna synthetase from escherichia coli.
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Authors
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C.Francklyn,
D.Harris,
D.Moras.
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Ref.
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J Mol Biol, 1994,
241,
275-277.
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PubMed id
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Secondary reference #2
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Title
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Primary structure of histidine-Trna synthetase and characterization of hiss transcripts.
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Authors
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R.Freedman,
B.Gibson,
D.Donovan,
K.Biemann,
S.Eisenbeis,
J.Parker,
P.Schimmel.
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Ref.
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J Biol Chem, 1985,
260,
10063-10068.
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PubMed id
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