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Thermus thermophilus HB8  TTHA0711
aspartyl-tRNA synthetase

Locus: 1:complement(674930..676672)
Synonym: TT0879
DNA Sequence:
(with up/down stream)
Amino Acid Sequence:
Stop Codon: TGA
DNA Length: 1740
AA Length: 580
Mol. Weight: 66038
pI: 5.9
Absorption coefficient: 69615
Number of Methionine: 10

Expression Plasmid:
Plasmid ID:Vector:Description:Met: Distribution from DNA BANK :
PC010711-41pET-11a 10available

Purification:
Expression Plasmid:Label:Purified Date:Yield (mg):

Plasmid for Gene Disruption:
BRCID:PDID:Vector:Marker Gene:Upstream:Downstream:
 PD010711-01 HTK  
Reference for HTK marker: Hoseki, J. et al. (1999) J Biochem, 126, 951-6.
Reference for gene disruption: Hashimoto, Y. et al. (2001) FEBS Lett, 506, 231-4.

Structure:
PDB_code:Deposit:
1L0W02/14/2002
1G5110/30/2000
1EFW02/10/2000
the most similar PDB entry:

Related Articles:
Moreno, A. et al., (2005) Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals Acta Crystallogr D Biol Crystallogr 61 :  789-92
Charron, C. et al., (2003) Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain EMBO J 22 :  1632-43
Charron, C. et al., (2002) Crystal contacts engineering of aspartyl-tRNA synthetase from Thermus thermophilus: effects on crystallizability Acta Crystallogr D Biol Crystallogr 58 :  1729-33
Lorber, B. et al., (2002) From conventional crystallization to better crystals from space: a review on pilot crystallogenesis studies with aspartyl-tRNA synthetases Acta Crystallogr D Biol Crystallogr 58 :  1674-80
Zhu, D. W. et al., (2001) Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermus thermophilus aspartyl-tRNA synthetase-1 Acta Crystallogr D Biol Crystallogr 57 :  552-8
Briand, C. et al., (2000) An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase J Mol Biol 299 :  1051-60
Becker, H. D. et al., (2000) Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase Biochemistry 39 :  3216-30
Briand, C. et al., (1998) Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems Acta Crystallogr D Biol Crystallogr 54 :  1382-6
Becker, H. D. et al., (1997) Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes Biochemistry 36 :  8785-97
Becker, H. D. et al., (1996) Identity of prokaryotic and eukaryotic tRNA(Asp) for aminoacylation by aspartyl-tRNA synthetase from Thermus thermophilus Biochemistry 35 :  7447-58
Poterszman, A. et al., (1994) Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase J Mol Biol 244 :  158-67
Poterszman, A. et al., (1993) Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases FEBS Lett 325 :  183-6